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Title: The structure of S . lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain

Abstract

The adenosine monoposphate-forming acyl-CoA synthetase enzymes catalyze a two-step reaction that involves the initial formation of an acyl adenylate that reacts in a second partial reaction to form a thioester between the acyl substrate and CoA. These enzymes utilize a Domain Alternation catalytic mechanism, whereby a ~110 residue C-terminal domain rotates by 140° to form distinct catalytic conformations for the two partial reactions. In this paper, the structure of an acetoacetyl-CoA synthetase (AacS) is presented that illustrates a novel aspect of this C-terminal domain. Specifically, several acetyl- and acetoacetyl-CoA synthetases contain a 30-residue extension on the C-terminus compared to other members of this family. Finally, whereas residues from this extension are disordered in prior structures, the AacS structure shows that residues from this extension may interact with key catalytic residues from the N-terminal domain.

Authors:
 [1];  [2];  [2];  [1]
+ Show Author Affiliations
  1. Hauptman-Woodward Institute, Buffalo New York 14203; Department of Structural Biology, University at Buffalo, Buffalo New York 14203
  2. Department of Microbiology, University of Georgia, Athens Georgia 30602
Publication Date:
Research Org.:
Hauptman-Woodward Inst., Buffalo, NY (United States); Univ. at Buffalo, NY (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)
OSTI Identifier:
1343103
Grant/Contract Number:  
AC02-76SF00515; GM-068440; GM062203
Resource Type:
Accepted Manuscript
Journal Name:
Proteins
Additional Journal Information:
Journal Volume: 83; Journal Issue: 3; Journal ID: ISSN 0887-3585
Publisher:
Wiley
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; enzymes; structural biology; adenylate-forming enzymes; ANL superfamily; lysine acetylation

Citation Formats

Mitchell, Carter A., Tucker, Alex C., Escalante-Semerena, Jorge C., and Gulick, Andrew M. The structure of S . lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain. United States: N. p., 2014. Web. doi:10.1002/prot.24738.
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Mitchell, Carter A., Tucker, Alex C., Escalante-Semerena, Jorge C., & Gulick, Andrew M. The structure of S . lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain. United States. https://doi.org/10.1002/prot.24738
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Mitchell, Carter A., Tucker, Alex C., Escalante-Semerena, Jorge C., and Gulick, Andrew M. Tue . "The structure of S . lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain". United States. https://doi.org/10.1002/prot.24738. https://www.osti.gov/servlets/purl/1343103.
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@article{osti_1343103,
title = {The structure of S . lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain},
author = {Mitchell, Carter A. and Tucker, Alex C. and Escalante-Semerena, Jorge C. and Gulick, Andrew M.},
abstractNote = {The adenosine monoposphate-forming acyl-CoA synthetase enzymes catalyze a two-step reaction that involves the initial formation of an acyl adenylate that reacts in a second partial reaction to form a thioester between the acyl substrate and CoA. These enzymes utilize a Domain Alternation catalytic mechanism, whereby a ~110 residue C-terminal domain rotates by 140° to form distinct catalytic conformations for the two partial reactions. In this paper, the structure of an acetoacetyl-CoA synthetase (AacS) is presented that illustrates a novel aspect of this C-terminal domain. Specifically, several acetyl- and acetoacetyl-CoA synthetases contain a 30-residue extension on the C-terminus compared to other members of this family. Finally, whereas residues from this extension are disordered in prior structures, the AacS structure shows that residues from this extension may interact with key catalytic residues from the N-terminal domain.},
doi = {10.1002/prot.24738},
journal = {Proteins},
number = 3,
volume = 83,
place = {United States},
year = {Tue Dec 09 00:00:00 EST 2014},
month = {Tue Dec 09 00:00:00 EST 2014}
}
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https://doi.org/10.1002/prot.24738
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Works referenced in this record:

Conformational Dynamics in the Acyl-CoA Synthetases, Adenylation Domains of Non-ribosomal Peptide Synthetases, and Firefly Luciferase
journal, October 2009

  • Gulick, Andrew M.
  • ACS Chemical Biology, Vol. 4, Issue 10, p. 811-827
  • DOI: 10.1021/cb900156h

Biochemical and Crystallographic Analysis of Substrate Binding and Conformational Changes in Acetyl-CoA Synthetase † , ‡
journal, June 2007

  • Reger, Albert S.; Carney, Jill M.; Gulick, Andrew M.
  • Biochemistry, Vol. 46, Issue 22
  • DOI: 10.1021/bi6026506

Structural Characterization of a 140° Domain Movement in the Two-Step Reaction Catalyzed by 4-Chlorobenzoate:CoA Ligase † ‡
journal, August 2008

  • Reger, Albert S.; Wu, Rui; Dunaway-Mariano, Debra
  • Biochemistry, Vol. 47, Issue 31
  • DOI: 10.1021/bi800696y

Structural and Functional Investigation of the Intermolecular Interaction between NRPS Adenylation and Carrier Protein Domains
journal, February 2012

Crystal Structure of DltA: IMPLICATIONS FOR THE REACTION MECHANISM OF NON-RIBOSOMAL PEPTIDE SYNTHETASE ADENYLATION DOMAINS
journal, September 2008

  • Yonus, Huma; Neumann, Piotr; Zimmermann, Stephan
  • Journal of Biological Chemistry, Vol. 283, Issue 47
  • DOI: 10.1074/jbc.M800557200

Mutagenesis Evidence that the Partial Reactions of Firefly Bioluminescence Are Catalyzed by Different Conformations of the Luciferase C-Terminal Domain †
journal, February 2005

  • Branchini, Bruce R.; Southworth, Tara L.; Murtiashaw, Martha H.
  • Biochemistry, Vol. 44, Issue 5
  • DOI: 10.1021/bi047903f

Crystal Structure of Firefly Luciferase in a Second Catalytic Conformation Supports a Domain Alternation Mechanism
journal, August 2012

  • Sundlov, Jesse A.; Fontaine, Danielle M.; Southworth, Tara L.
  • Biochemistry, Vol. 51, Issue 33
  • DOI: 10.1021/bi300934s

Sir2-Dependent Activation of Acetyl-CoA Synthetase by Deacetylation of Active Lysine
journal, December 2002

The 1.75 Å Crystal Structure of Acetyl-CoA Synthetase Bound to Adenosine-5‘-propylphosphate and Coenzyme A †
journal, March 2003

  • Gulick, Andrew M.; Starai, Vincent J.; Horswill, Alexander R.
  • Biochemistry, Vol. 42, Issue 10, p. 2866-2873
  • DOI: 10.1021/bi0271603

Crystal Structure of Yeast Acetyl-Coenzyme A Synthetase in Complex with AMP
journal, February 2004

  • Jogl, Gerwald; Tong, Liang
  • Biochemistry, Vol. 43, Issue 6, p. 1425-1431
  • DOI: 10.1021/bi035911a

Characterization of the Propionyl-CoA Synthetase (PrpE) Enzyme of Salmonella enterica :  Residue Lys592 Is Required for Propionyl-AMP Synthesis †
journal, February 2002

  • Horswill, Alexander R.; Escalante-Semerena, Jorge C.
  • Biochemistry, Vol. 41, Issue 7
  • DOI: 10.1021/bi015647q

[20] Processing of X-ray diffraction data collected in oscillation mode
book, January 1997

PHENIX: a comprehensive Python-based system for macromolecular structure solution
journal, January 2010

  • Adams, Paul D.; Afonine, Pavel V.; Bunkóczi, Gábor
  • Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 2, p. 213-221
  • DOI: 10.1107/S0907444909052925

MolProbity : all-atom structure validation for macromolecular crystallography
journal, December 2009

  • Chen, Vincent B.; Arendall, W. Bryan; Headd, Jeffrey J.
  • Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 1
  • DOI: 10.1107/S0907444909042073

Overview of the CCP 4 suite and current developments
journal, March 2011

  • Winn, Martyn D.; Ballard, Charles C.; Cowtan, Kevin D.
  • Acta Crystallographica Section D Biological Crystallography, Vol. 67, Issue 4
  • DOI: 10.1107/S0907444910045749

Dali server: conservation mapping in 3D
journal, May 2010

  • Holm, Liisa; Rosenstr�m, P�ivi
  • Nucleic Acids Research, Vol. 38, Issue suppl_2
  • DOI: 10.1093/nar/gkq366
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