Evolutionarily conserved linkage between enzyme fold, flexibility, and catalysis

Ramanathan, Arvind; Agarwal, Pratul K

doi:10.1371/journal.pbio.1001193

Title: Evolutionarily conserved linkage between enzyme fold, flexibility, and catalysis

Journal Article · Sat Jan 01 00:00:00 EST 2011 · PLoS biology (Online)

DOI:https://doi.org/10.1371/journal.pbio.1001193· OSTI ID:1049058

Ramanathan, Arvind ^[1]; Agarwal, Pratul K ^[1]

ORNL

Proteins are intrinsically flexible molecules. The role of internal motions in a protein's designated function is widely debated. The role of protein structure in enzyme catalysis is well established, and conservation of structural features provides vital clues to their role in function. Recently, it has been proposed that the protein function may involve multiple conformations: the observed deviations are not random thermodynamic fluctuations; rather, flexibility may be closely linked to protein function, including enzyme catalysis. We hypothesize that the argument of conservation of important structural features can also be extended to identification of protein flexibility in interconnection with enzyme function. Three classes of enzymes (prolyl-peptidyl isomerase, oxidoreductase, and nuclease) that catalyze diverse chemical reactions have been examined using detailed computational modeling. For each class, the identification and characterization of the internal protein motions coupled to the chemical step in enzyme mechanisms in multiple species show identical enzyme conformational fluctuations. In addition to the active-site residues, motions of protein surface loop regions (>10 away) are observed to be identical across species, and networks of conserved interactions/residues connect these highly flexible surface regions to the active-site residues that make direct contact with substrates. More interestingly, examination of reaction-coupled motions in non-homologous enzyme systems (with no structural or sequence similarity) that catalyze the same biochemical reaction shows motions that induce remarkably similar changes in the enzyme substrate interactions during catalysis. The results indicate that the reaction-coupled flexibility is a conserved aspect of the enzyme molecular architecture. Protein motions in distal areas of homologous and non-homologous enzyme systems mediate similar changes in the active-site enzyme substrate interactions, thereby impacting the mechanism of catalyzed chemistry. These results have implications for understanding the mechanism of allostery, and for protein engineering and drug design.

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Research Organization:: Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Oak Ridge Leadership Computing Facility (OLCF); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). National Center for Computational Sciences (NCCS)

Sponsoring Organization:: USDOE Office of Science (SC); USDOE Laboratory Directed Research and Development (LDRD) Program

DOE Contract Number:: DE-AC05-00OR22725

OSTI ID:: 1049058

Journal Information:: PLoS biology (Online), Vol. 9, Issue 11; ISSN 1545-7885

Country of Publication:: United States

Language:: English

References (80)

Is one solution good enough? Furnham, Nicholas; Blundell, Tom L.; DePristo, Mark A. Nature Structural & Molecular Biology, Vol. 13, Issue 3 https://doi.org/10.1038/nsmb0306-184	journal	March 2006
Relating Protein Motion to Catalysis Hammes-Schiffer, Sharon; Benkovic, Stephen J. Annual Review of Biochemistry, Vol. 75, Issue 1 https://doi.org/10.1146/annurev.biochem.75.103004.142800	journal	June 2006
An NMR Perspective on Enzyme Dynamics Boehr, David D.; Dyson, H. Jane; Wright, Peter E. Chemical Reviews, Vol. 106, Issue 8 https://doi.org/10.1021/cr050312q	journal	August 2006
Dynamical Contributions to Enzyme Catalysis: Critical Tests of A Popular Hypothesis Olsson, Mats H. M.; Parson, William W.; Warshel, Arieh Chemical Reviews, Vol. 106, Issue 5 https://doi.org/10.1021/cr040427e	journal	May 2006
A hierarchy of timescales in protein dynamics is linked to enzyme catalysis Henzler-Wildman, Katherine A.; Lei, Ming; Thai, Vu Nature, Vol. 450, Issue 7171 https://doi.org/10.1038/nature06407	journal	November 2007
A 21st century revisionist's view at a turning point in enzymology Nagel, Zachary D.; Klinman, Judith P. Nature Chemical Biology, Vol. 5, Issue 8 https://doi.org/10.1038/nchembio.204	journal	July 2009
Enzyme millisecond conformational dynamics do not catalyze the chemical step Pisliakov, A. V.; Cao, J.; Kamerlin, S. C. L. Proceedings of the National Academy of Sciences, Vol. 106, Issue 41 https://doi.org/10.1073/pnas.0909150106	journal	September 2009
Application of a Theory of Enzyme Specificity to Protein Synthesis Koshland, D. E. Proceedings of the National Academy of Sciences, Vol. 44, Issue 2 https://doi.org/10.1073/pnas.44.2.98	journal	February 1958
Free-Energy Landscape of Enzyme Catalysis ^† Benkovic, Stephen J.; Hammes, Gordon G.; Hammes-Schiffer, Sharon Biochemistry, Vol. 47, Issue 11 https://doi.org/10.1021/bi800049z	journal	March 2008
The Flexibility of a Distant Loop Modulates Active Site Motion and Product Release in Ribonuclease A Doucet, Nicolas; Watt, Eric D.; Loria, J. Patrick Biochemistry, Vol. 48, Issue 30 https://doi.org/10.1021/bi900830g	journal	August 2009
Protein Dynamics in Enzymatic Catalysis: Exploration of Dihydrofolate Reductase Radkiewicz, Jennifer L.; Brooks, Charles L. Journal of the American Chemical Society, Vol. 122, Issue 2 https://doi.org/10.1021/ja9913838	journal	January 2000
Network of coupled promoting motions in enzyme catalysis Agarwal, P. K.; Billeter, S. R.; Rajagopalan, P. T. R. Proceedings of the National Academy of Sciences, Vol. 99, Issue 5, p. 2794-2799 https://doi.org/10.1073/pnas.052005999	journal	February 2002
Reaction-Path Energetics and Kinetics of the Hydride Transfer Reaction Catalyzed by Dihydrofolate Reductase ^† Garcia-Viloca, Mireia; Truhlar, Donald G.; Gao, Jiali Biochemistry, Vol. 42, Issue 46 https://doi.org/10.1021/bi034824f	journal	November 2003
Rate-promoting vibrations and coupled hydrogen–electron transfer reactions in the condensed phase: A model for enzymatic catalysis Mincer, Joshua S.; Schwartz, Steven D. The Journal of Chemical Physics, Vol. 120, Issue 16 https://doi.org/10.1063/1.1690239	journal	April 2004
Solvation, Reorganization Energy, and Biological Catalysis Cannon, William R.; Benkovic, Stephen J. Journal of Biological Chemistry, Vol. 273, Issue 41 https://doi.org/10.1074/jbc.273.41.26257	journal	October 1998
Enzymatic transition states and dynamic motion in barrier crossing Schwartz, Steven D.; Schramm, Vern L. Nature Chemical Biology, Vol. 5, Issue 8 https://doi.org/10.1038/nchembio.202	journal	July 2009
Identification of a Protein-Promoting Vibration in the Reaction Catalyzed by Horse Liver Alcohol Dehydrogenase Caratzoulas, Stavros; Mincer, Joshua S.; Schwartz, Steven D. Journal of the American Chemical Society, Vol. 124, Issue 13 https://doi.org/10.1021/ja017146y	journal	April 2002
Single Molecule Studies of Enzyme Mechanisms Smiley, R. Derike; Hammes, Gordon G. Chemical Reviews, Vol. 106, Issue 8 https://doi.org/10.1021/cr0502955	journal	August 2006
Enzyme Dynamics During Catalysis Eisenmesser, E. Z. Science, Vol. 295, Issue 5559 https://doi.org/10.1126/science.1066176	journal	February 2002
Hidden alternative structures of proline isomerase essential for catalysis Fraser, James S.; Clarkson, Michael W.; Degnan, Sheena C. Nature, Vol. 462, Issue 7273 https://doi.org/10.1038/nature08615	journal	December 2009
Effect of Cofactor Binding and Loop Conformation on Side Chain Methyl Dynamics in Dihydrofolate Reductase ^† Schnell, Jason R.; Dyson, H. Jane; Wright, Peter E. Biochemistry, Vol. 43, Issue 2 https://doi.org/10.1021/bi035464z	journal	January 2004
The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis Boehr, D. D.; McElheny, D.; Dyson, H. J. Science, Vol. 313, Issue 5793, p. 1638-1642 https://doi.org/10.1126/science.1130258	journal	September 2006
Conformation Coupled Enzyme Catalysis: Single-Molecule and Transient Kinetics Investigation of Dihydrofolate Reductase ^† Antikainen, Nina M.; Smiley, R. Derike; Benkovic, Stephen J. Biochemistry, Vol. 44, Issue 51 https://doi.org/10.1021/bi051378i	journal	December 2005
Protein Dynamics and Enzymatic Catalysis: Investigating the Peptidyl−Prolyl Cis−Trans Isomerization Activity of Cyclophilin A ^† Agarwal, Pratul K.; Geist, Al; Gorin, Andrey Biochemistry, Vol. 43, Issue 33 https://doi.org/10.1021/bi0495228	journal	August 2004
Role of Protein Dynamics in Reaction Rate Enhancement by Enzymes Agarwal, Pratul K. Journal of the American Chemical Society, Vol. 127, Issue 43 https://doi.org/10.1021/ja055251s	journal	November 2005
A Perspective on Enzyme Catalysis Benkovic, S. J. Science, Vol. 301, Issue 5637 https://doi.org/10.1126/science.1085515	journal	August 2003
Nuclear Quantum Effects and Enzyme Dynamics in Dihydrofolate Reductase Catalysis Agarwal, Pratul K.; Billeter, Salomon R.; Hammes-Schiffer, Sharon The Journal of Physical Chemistry B, Vol. 106, Issue 12 https://doi.org/10.1021/jp020190v	journal	March 2002
Correlated motion and the effect of distal mutations in dihydrofolate reductase Rod, T. H.; Radkiewicz, J. L.; Brooks, C. L. Proceedings of the National Academy of Sciences, Vol. 100, Issue 12 https://doi.org/10.1073/pnas.1230801100	journal	May 2003
Protein Motions Promote Catalysis Tousignant, Audrey; Pelletier, Joelle N. Chemistry & Biology, Vol. 11, Issue 8 https://doi.org/10.1016/j.chembiol.2004.06.007	journal	August 2004
How Enzymes Work: Analysis by Modern Rate Theory and Computer Simulations Garcia-Viloca, M. Science, Vol. 303, Issue 5655 https://doi.org/10.1126/science.1088172	journal	January 2004
Slow Conformational Motions That Favor Sub-picosecond Motions Important for Catalysis Pineda, J. R. Exequiel T.; Antoniou, Dimitri; Schwartz, Steven D. The Journal of Physical Chemistry B, Vol. 114, Issue 48 https://doi.org/10.1021/jp1071296	journal	December 2010
Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands Boehr, D. D.; McElheny, D.; Dyson, H. J. Proceedings of the National Academy of Sciences, Vol. 107, Issue 4 https://doi.org/10.1073/pnas.0914163107	journal	January 2010
Intrinsic dynamics of an enzyme underlies catalysis Eisenmesser, Elan Z.; Millet, Oscar; Labeikovsky, Wladimir Nature, Vol. 438, Issue 7064 https://doi.org/10.1038/nature04105	journal	November 2005
Bulk-solvent and hydration-shell fluctuations, similar to - and -fluctuations in glasses, control protein motions and functions Fenimore, P. W.; Frauenfelder, H.; McMahon, B. H. Proceedings of the National Academy of Sciences, Vol. 101, Issue 40 https://doi.org/10.1073/pnas.0405573101	journal	September 2004
Electrostatic Contributions to Binding of Transition State Analogues Can Be Very Different from the Corresponding Contributions to Catalysis: Phenolates Binding to the Oxyanion Hole of Ketosteroid Isomerase ^† Warshel, Arieh; Sharma, Pankaz K.; Chu, Zhen T. Biochemistry, Vol. 46, Issue 6 https://doi.org/10.1021/bi061752u	journal	February 2007
Electrostatic Basis for Enzyme Catalysis Warshel, Arieh; Sharma, Pankaz K.; Kato, Mitsunori Chemical Reviews, Vol. 106, Issue 8 https://doi.org/10.1021/cr0503106	journal	August 2006
Chemical Basis for Enzyme Catalysis Bruice, Thomas C.; Benkovic, Stephen J. Biochemistry, Vol. 39, Issue 21 https://doi.org/10.1021/bi0003689	journal	May 2000
Divergent Evolution of Enzymatic Function: Mechanistically Diverse Superfamilies and Functionally Distinct Suprafamilies Gerlt, John A.; Babbitt, Patricia C. Annual Review of Biochemistry, Vol. 70, Issue 1 https://doi.org/10.1146/annurev.biochem.70.1.209	journal	June 2001
Evolution of enzyme superfamilies Glasner, M.; Gerlt, J.; Babbitt, P. Current Opinion in Chemical Biology, Vol. 10, Issue 5 https://doi.org/10.1016/j.cbpa.2006.08.012	journal	October 2006
How do enzymes work? Kraut, J. Science, Vol. 242, Issue 4878 https://doi.org/10.1126/science.3051385	journal	October 1988
Convergent Dynamics in the Protease Enzymatic Superfamily Carnevale, Vincenzo; Raugei, Simone; Micheletti, Cristian Journal of the American Chemical Society, Vol. 128, Issue 30 https://doi.org/10.1021/ja060896t	journal	August 2006
Proteins with Similar Architecture Exhibit Similar Large-Scale Dynamic Behavior Keskin, O.; Jernigan, R. L.; Bahar, I. Biophysical Journal, Vol. 78, Issue 4 https://doi.org/10.1016/S0006-3495(00)76756-7	journal	April 2000
Evolutionary conservation of protein vibrational dynamics Maguid, Sandra; Fernandez-Alberti, Sebastian; Echave, Julian Gene, Vol. 422, Issue 1-2 https://doi.org/10.1016/j.gene.2008.06.002	journal	October 2008
Correspondences between low-energy modes in enzymes: Dynamics-based alignment of enzymatic functional families Zen, Andrea; Carnevale, Vincenzo; Lesk, Arthur M. Protein Science, Vol. 17, Issue 5 https://doi.org/10.1110/ps.073390208	journal	May 2008
Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases FanghÃ¤nel, JÃ¶rg Frontiers in Bioscience, Vol. 9, Issue 1-3 https://doi.org/10.2741/1494	journal	January 2004
Structural insights into the catalytic mechanism of cyclophilin A Howard, Bruce R.; Vajdos, Felix F.; Li, Su Nature Structural & Molecular Biology, Vol. 10, Issue 6 https://doi.org/10.1038/nsb927	journal	May 2003
What Is So Special about Arg 55 in the Catalysis of Cyclophilin A? Insights from Hybrid QM/MM Simulations Li, Guohui; Cui, Qiang Journal of the American Chemical Society, Vol. 125, Issue 49 https://doi.org/10.1021/ja0367851	journal	December 2003
Similarities between principal components of protein dynamics and random diffusion Hess, Berk Physical Review E, Vol. 62, Issue 6 https://doi.org/10.1103/PhysRevE.62.8438	journal	December 2000
Structural and Functional Analysis of the Mitotic Rotamase Pin1 Suggests Substrate Recognition Is Phosphorylation Dependent Ranganathan, Rama; Lu, Kun Ping; Hunter, Tony Cell, Vol. 89, Issue 6 https://doi.org/10.1016/S0092-8674(00)80273-1	journal	June 1997
Structure and Dynamics of Pin1 During Catalysis by NMR Labeikovsky, Wladimir; Eisenmesser, Elan Z.; Bosco, Daryl A. Journal of Molecular Biology, Vol. 367, Issue 5 https://doi.org/10.1016/j.jmb.2007.01.049	journal	April 2007
Functionally Important Residues in the Peptidyl-prolyl Isomerase Pin1 Revealed by Unigenic Evolution Behrsin, C. D.; Bailey, M. L.; Bateman, K. S. Journal of Molecular Biology, Vol. 365, Issue 4 https://doi.org/10.1016/j.jmb.2006.10.078	journal	January 2007
Loop and Subdomain Movements in the Mechanism of Escherichia coli Dihydrofolate Reductase: Crystallographic Evidence ^† ^, ^‡ Sawaya, Michael R.; Kraut, Joseph Biochemistry, Vol. 36, Issue 3 https://doi.org/10.1021/bi962337c	journal	January 1997
Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase Wang, L.; Goodey, N. M.; Benkovic, S. J. Proceedings of the National Academy of Sciences, Vol. 103, Issue 43 https://doi.org/10.1073/pnas.0606976103	journal	October 2006
Multiple Conformational Changes in Enzyme Catalysis ^† Hammes, Gordon G. Biochemistry, Vol. 41, Issue 26 https://doi.org/10.1021/bi0260839	journal	July 2002
Searching Sequence Space: Two Different Approaches to Dihydrofolate Reductase Catalysis Howell, Elizabeth E. ChemBioChem, Vol. 6, Issue 4 https://doi.org/10.1002/cbic.200400237	journal	April 2005
Crystal Structure of a Type II Dihydrofolate Reductase Catalytic Ternary Complex ^† Krahn, Joseph M.; Jackson, Michael R.; DeRose, Eugene F. Biochemistry, Vol. 46, Issue 51 https://doi.org/10.1021/bi701532r	journal	December 2007
The Tail Wagging the Dog: Insights into Catalysis in R67 Dihydrofolate Reductase Kamath, Ganesh; Howell, Elizabeth E.; Agarwal, Pratul K. Biochemistry, Vol. 49, Issue 42 https://doi.org/10.1021/bi1007222	journal	October 2010
Evaluation of the factors influencing reactivity and stereospecificity in NAD(P)H dependent dehydrogenase enzymes Almarsson, Orn; Bruice, Thomas C. Journal of the American Chemical Society, Vol. 115, Issue 6 https://doi.org/10.1021/ja00059a005	journal	March 1993
Evidence for Flexibility in the Function of Ribonuclease A ^† Cole, Roger; Loria, J. Patrick Biochemistry, Vol. 41, Issue 19 https://doi.org/10.1021/bi025655m	journal	May 2002
Refined Crystal Structures of Native Human Angiogenin and Two Active Site Variants: Implications for the Unique Functional Properties of an Enzyme Involved in Neovascularisation During Tumour Growth Leonidas, Demetres D.; Shapiro, Robert; Allen, Simon C. Journal of Molecular Biology, Vol. 285, Issue 3 https://doi.org/10.1006/jmbi.1998.2378	journal	January 1999
Molecular Dynamics Simulation of Bovine Pancreatic Ribonuclease A−CpA and Transition State-like Complexes Formoso, Elena; Matxain, Jon M.; Lopez, Xabier The Journal of Physical Chemistry B, Vol. 114, Issue 21 https://doi.org/10.1021/jp909004y	journal	June 2010
Enzyme Dynamics along the Reaction Coordinate: Critical Role of a Conserved Residue Kovrigin, Evgenii L.; Loria, J. Patrick Biochemistry, Vol. 45, Issue 8 https://doi.org/10.1021/bi0525066	journal	February 2006
Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families Lockless, S. W. Science, Vol. 286, Issue 5438 https://doi.org/10.1126/science.286.5438.295	journal	October 1999
Discovering Conformational Sub-States Relevant to Protein Function Ramanathan, Arvind; Savol, Andrej J.; Langmead, Christopher J. PLoS ONE, Vol. 6, Issue 1 https://doi.org/10.1371/journal.pone.0015827	journal	January 2011
Barriers to Hydride Transfer in Wild Type and Mutant Dihydrofolate Reductase from E. c oli Thorpe, Ian F.; Brooks, Charles L. The Journal of Physical Chemistry B, Vol. 107, Issue 50 https://doi.org/10.1021/jp035734n	journal	December 2003
Role of Lys-32 Residues in R67 Dihydrofolate Reductase Probed by Asymmetric Mutations Hicks, Stephanie N.; Smiley, R. Derike; Stinnett, Lori G. Journal of Biological Chemistry, Vol. 279, Issue 45 https://doi.org/10.1074/jbc.M404484200	journal	August 2004
Surface Sites for Engineering Allosteric Control in Proteins Lee, J.; Natarajan, M.; Nashine, V. C. Science, Vol. 322, Issue 5900 https://doi.org/10.1126/science.1159052	journal	October 2008
Effects of a Distal Mutation on Active Site Chemistry ^† Wang, Lin; Tharp, Scott; Selzer, Tzvia Biochemistry, Vol. 45, Issue 5 https://doi.org/10.1021/bi0518242	journal	February 2006
The mechanism of rate-limiting motions in enzyme function Watt, E. D.; Shimada, H.; Kovrigin, E. L. Proceedings of the National Academy of Sciences, Vol. 104, Issue 29 https://doi.org/10.1073/pnas.0702551104	journal	July 2007
Freezing a Single Distal Motion in Dihydrofolate Reductase Sergi, Alessandro; Watney, James B.; Wong, Kim F. The Journal of Physical Chemistry B, Vol. 110, Issue 5 https://doi.org/10.1021/jp056939u	journal	February 2006
Conformational Substates Modulate Hydride Transfer in Dihydrofolate Reductase Thorpe, Ian F.; Brooks, Charles L. Journal of the American Chemical Society, Vol. 127, Issue 37 https://doi.org/10.1021/ja053558l	journal	September 2005
The Amber biomolecular simulation programs Case, David A.; Cheatham, Thomas E.; Darden, Tom Journal of Computational Chemistry, Vol. 26, Issue 16 https://doi.org/10.1002/jcc.20290	journal	January 2005
Cis/trans isomerization in HIV-1 capsid protein catalyzed by cyclophilin A: Insights from computational and theoretical studies Agarwal, Pratul K. Proteins: Structure, Function, and Bioinformatics, Vol. 56, Issue 3 https://doi.org/10.1002/prot.20135	journal	May 2004
Dynamics of enzymatic reactions. Warshel, A. Proceedings of the National Academy of Sciences, Vol. 81, Issue 2 https://doi.org/10.1073/pnas.81.2.444	journal	January 1984
Evaluation of the configurational entropy for proteins: application to molecular dynamics simulations of an α-helix Levy, Ronald M.; Karplus, Martin; Kushick, Joseph Macromolecules, Vol. 17, Issue 7 https://doi.org/10.1021/ma00137a013	journal	July 1984
An Online Approach for Mining Collective Behaviors from Molecular Dynamics Simulations Ramanathan, Arvind; Agarwal, Pratul K.; Kurnikova, Maria Journal of Computational Biology, Vol. 17, Issue 3 https://doi.org/10.1089/cmb.2009.0167	journal	March 2010
Computational Identification of Slow Conformational Fluctuations in Proteins Ramanathan, Arvind; Agarwal, Pratul K. The Journal of Physical Chemistry B, Vol. 113, Issue 52 https://doi.org/10.1021/jp9077213	journal	December 2009
CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Thompson, Julie D.; Higgins, Desmond G.; Gibson, Toby J. Nucleic Acids Research, Vol. 22, Issue 22, p. 4673-4680 https://doi.org/10.1093/nar/22.22.4673	journal	January 1994
Molecular Dynamics Simulations of Protein G Challenge NMR-Derived Correlated Backbone Motions Lange, Oliver F.; Grubmüller, Helmut; de Groot, Bert L. Angewandte Chemie International Edition, Vol. 44, Issue 22 https://doi.org/10.1002/anie.200462957	journal	May 2005
Assessing equilibration and convergence in biomolecular simulations Smith, Lorna J.; Daura, Xavier; van Gunsteren, Wilfred F. Proteins: Structure, Function, and Genetics, Vol. 48, Issue 3 https://doi.org/10.1002/prot.10144	journal	June 2002

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Title: Evolutionarily conserved linkage between enzyme fold, flexibility, and catalysis

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