Conformational Changes of the Clamp of the Protein Translocation ATPase SecA

Chen, Yu; Bauer, Benedikt W.; Rapoport, Tom A.; Gumbart, James C.

doi:10.1016/j.jmb.2015.05.003

Title: Conformational Changes of the Clamp of the Protein Translocation ATPase SecA

Authors:

Chen, Yu; Bauer, Benedikt W.; Rapoport, Tom A.; Gumbart, James C. ^[1]; GIT) ^[2]

Harvard-Med
(

Publication Date:: Wed Jul 01 00:00:00 EDT 2015

Research Org.:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Org.:: NIHHHMI; USDOE

OSTI Identifier:: 1184858

Alternate Identifier(s):: OSTI ID: 1359354

Grant/Contract Number:: AC02-06CH11357

Resource Type:: Accepted Manuscript

Journal Name:: J. Mol. Biol.

Additional Journal Information:: Journal Volume: 427; Journal Issue: (14) ; 07, 2015

Country of Publication:: United States

Language:: ENGLISH

Citation Formats


                    Chen, Yu, Bauer, Benedikt W., Rapoport, Tom A., Gumbart, James C., and GIT). Conformational Changes of the Clamp of the Protein Translocation ATPase SecA.  United States: N. p., 2015. 
Web.  doi:10.1016/j.jmb.2015.05.003.

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                    Chen, Yu, Bauer, Benedikt W., Rapoport, Tom A., Gumbart, James C., & GIT). Conformational Changes of the Clamp of the Protein Translocation ATPase SecA.  United States.  https://doi.org/10.1016/j.jmb.2015.05.003

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                    Chen, Yu, Bauer, Benedikt W., Rapoport, Tom A., Gumbart, James C., and GIT). Wed .  
"Conformational Changes of the Clamp of the Protein Translocation ATPase SecA".  United States.  https://doi.org/10.1016/j.jmb.2015.05.003.  https://www.osti.gov/servlets/purl/1184858.

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@article{osti_1184858,

  title        = {Conformational Changes of the Clamp of the Protein Translocation ATPase SecA},

  author       = {Chen, Yu and Bauer, Benedikt W. and Rapoport, Tom A. and Gumbart, James C. and GIT)},

  abstractNote = {},

  doi          = {10.1016/j.jmb.2015.05.003},

  journal      = {J. Mol. Biol.},

  number       = (14) ; 07, 2015,

  volume       = 427,

  place        = {United States},

  year         = {Wed Jul 01 00:00:00 EDT 2015},

  month        = {Wed Jul 01 00:00:00 EDT 2015}

}

Copy to clipboard

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https://doi.org/10.1016/j.jmb.2015.05.003

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Cited by: 21 works

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Works referenced in this record:

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Rapoport, Tom A.
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Mechanisms of Sec61/SecY-Mediated Protein Translocation Across Membranes
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A large conformational change of the translocation ATPase SecA
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A Novel Dimer Interface and Conformational Changes Revealed by an X-ray Structure of B. subtilis SecA
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Zimmer, Jochen; Li, Weikai; Rapoport, Tom A.
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Structure of Dimeric SecA, the Escherichia coli Preprotein Translocase Motor
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Papanikolau, Yannis; Papadovasilaki, Maria; Ravelli, Raimond B. G.
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Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase
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Sharma, V.; Arockiasamy, A.; Ronning, D. R.
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Crystal Structure of the Translocation ATPase SecA from Thermus thermophilus Reveals a Parallel, Head-to-Head Dimer
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Vassylyev, Dmitry G.; Mori, Hiroyuki; Vassylyeva, Marina N.
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Conformational Flexibility and Peptide Interaction of the Translocation ATPase SecA
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Zimmer, Jochen; Rapoport, Tom A.
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Structure of a complex of the ATPase SecA and the protein-translocation channel
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A role for the two-helix finger of the SecA ATPase in protein translocation
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A “Push and Slide” Mechanism Allows Sequence-Insensitive Translocation of Secretory Proteins by the SecA ATPase
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ATPase Active-Site Electrostatic Interactions Control the Global Conformation of the 100 kDa SecA Translocase
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Kim, Dorothy M.; Zheng, Haiyan; Huang, Yuanpeng J.
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Mapping polypeptide interactions of the SecA ATPase during translocation
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Analysis of Polypeptide Movement in the SecY Channel during SecA-mediated Protein Translocation
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Works referencing / citing this record:

Protein export through the bacterial Sec pathway
journal, November 2016

Tsirigotaki, Alexandra; De Geyter, Jozefien; Šoštaric´, Nikolina
Nature Reviews Microbiology, Vol. 15, Issue 1
DOI: 10.1038/nrmicro.2016.161

Structure of the substrate-engaged SecA-SecY protein translocation machine
journal, June 2019

Ma, Chengying; Wu, Xiaofei; Sun, Dongjie
Nature Communications, Vol. 10, Issue 1
DOI: 10.1038/s41467-019-10918-2

Preprotein mature domains contain translocase targeting signals that are essential for secretion
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Chatzi, Katerina E.; Sardis, Marios Frantzeskos; Tsirigotaki, Alexandra
Journal of Cell Biology, Vol. 216, Issue 5
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The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria
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Cranford-Smith, Tamar; Huber, Damon
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Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis
journal, October 2018

Chada, Nagaraju; Chattrakun, Kanokporn; Marsh, Brendan P.
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Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2
journal, December 2015

Swanson, Stephanie; Ioerger, Thomas R.; Rigel, Nathan W.
Journal of Bacteriology, Vol. 198, Issue 4
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Protein translocation by the SecA ATPase occurs by a power‐stroke mechanism
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Catipovic, Marco A.; Bauer, Benedikt W.; Loparo, Joseph J.
The EMBO Journal, Vol. 38, Issue 9
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The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity
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Jamshad, Mohammed; Knowles, Timothy J.; White, Scott A.
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Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2
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Miriam, Braunstein,; K., Miller, Brittany; W., Rigel, Nathan
The University of North Carolina at Chapel Hill University Libraries
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Structure of the substrate-engaged SecA-SecY protein translocation machine
journal, June 2019

Ma, Chengying; Wu, Xiaofei; Sun, Dongjie
Nature Communications, Vol. 10, Issue 1
DOI: 10.1038/s41467-019-10918-2

Novel Sequence Feature of SecA Translocase Protein Unique to the Thermophilic Bacteria: Bioinformatics Analyses to Investigate Their Potential Roles
journal, December 2019

Khadka, Bijendra; Persaud, Dhillon; Gupta, Radhey S.
Microorganisms, Vol. 8, Issue 1
DOI: 10.3390/microorganisms8010059

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A LARGE CONFORMATIONAL CHANGE OF THE TRANSLOCATION ATPASE SECA

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No abstract prepared.
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Conformational Flexibility and Peptide Interaction of the Translocation ATPase SecA

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Most proteins are secreted from bacteria by the interaction of the cytoplasmic SecA ATPase with a membrane channel, formed by the heterotrimeric SecY complex. Here we report the crystal structure of SecA bound to the SecY complex, with a maximum resolution of 4.5 {angstrom}(A), obtained for components from Thermotoga maritima. One copy of SecA in an intermediate state of ATP hydrolysis is bound to one molecule of the SecY complex. Both partners undergo important conformational changes on interaction. The polypeptide-cross-linking domain of SecA makes a large conformational change that could capture the translocation substrate in a 'clamp'. Polypeptide movement throughmore »« less
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The SecA ATPase forms a functional complex with the protein-conducting SecY channel to translocate polypeptides across the bacterial cell membrane. SecA recognizes the translocation substrate and catalyzes its unidirectional movement through the SecY channel. The recent crystal structure of the Thermotoga maritima SecA-SecYEG complex shows the ATPase in a conformation where the nucleotide-binding domains (NBDs) have closed around a bound ADP-BeFx complex and SecA's polypeptide-binding clamp is shut. Here, we present the crystal structure of T. maritima SecA in isolation, determined in its ADP-bound form at 3.1 {angstrom} resolution. SecA alone has a drastically different conformation in which the nucleotide-bindingmore »« less
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Most proteins are secreted from bacteria by the interaction of the cytoplasmic SecA ATPase with a membrane channel, formed by the heterotrimeric SecY complex. Here we report the crystal structure of SecA bound to the SecY complex, with a maximum resolution of 4.5 {angstrom}, obtained for components from Thermotoga maritima. One copy of SecA in an intermediate state of ATP hydrolysis is bound to one molecule of the SecY complex. Both partners undergo important conformational changes on interaction. The polypeptide-cross-linking domain of SecA makes a large conformational change that could capture the translocation substrate in a 'clamp'. Polypeptide movement throughmore »« less
https://doi.org/10.1038/nature07335

Similar Records

Title: Conformational Changes of the Clamp of the Protein Translocation ATPase SecA

Citation Formats

Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes journal, November 2007

Mechanisms of Sec61/SecY-Mediated Protein Translocation Across Membranes journal, June 2012

Protein Translocation Across the Bacterial Cytoplasmic Membrane journal, June 2008

The Sec protein-translocation pathway journal, October 2001

The Sec translocon mediated protein transport in prokaryotes and eukaryotes journal, March 2014

BiP Acts as a Molecular Ratchet during Posttranslational Transport of Prepro-α Factor across the ER Membrane journal, May 1999

SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion journal, September 1994

Structure and function of SecA, the preprotein translocase nanomotor journal, November 2004

Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA journal, September 2002

A large conformational change of the translocation ATPase SecA journal, July 2004

A Novel Dimer Interface and Conformational Changes Revealed by an X-ray Structure of B. subtilis SecA journal, December 2006

Structure of Dimeric SecA, the Escherichia coli Preprotein Translocase Motor journal, March 2007

Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase journal, February 2003

Crystal Structure of the Translocation ATPase SecA from Thermus thermophilus Reveals a Parallel, Head-to-Head Dimer journal, December 2006

Conformational Flexibility and Peptide Interaction of the Translocation ATPase SecA journal, December 2009

Structure of a complex of the ATPase SecA and the protein-translocation channel journal, October 2008

A role for the two-helix finger of the SecA ATPase in protein translocation journal, October 2008

A “Push and Slide” Mechanism Allows Sequence-Insensitive Translocation of Secretory Proteins by the SecA ATPase journal, June 2014

ATPase Active-Site Electrostatic Interactions Control the Global Conformation of the 100 kDa SecA Translocase journal, February 2013

Mapping polypeptide interactions of the SecA ATPase during translocation journal, November 2009

A Recipe for the Computation of the Free Energy Barrier and the Lowest Free Energy Path of Concerted Reactions † journal, April 2005

[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

Features and development of Coot journal, March 2010

Towards automated crystallographic structure refinement with phenix.refine journal, March 2012

Collaboration gets the most out of software journal, September 2013

Optimization of the Additive CHARMM All-Atom Protein Force Field Targeting Improved Sampling of the Backbone ϕ, ψ and Side-Chain χ 1 and χ 2 Dihedral Angles journal, August 2012

VMD: Visual molecular dynamics journal, February 1996

Scalable molecular dynamics with NAMD journal, January 2005

Calculating free energies using average force journal, November 2001

Exploring Multidimensional Free Energy Landscapes Using Time-Dependent Biases on Collective Variables journal, December 2009

Analysis of Polypeptide Movement in the SecY Channel during SecA-mediated Protein Translocation journal, June 2008

X-Ray Diffraction data from Protein translocation ATPase SecA, source of 4YS0 structure dataset, January 2015

X-Ray Diffraction data from Protein translocation ATPase SecA, source of 4YS0 structure dataset, January 2015

Protein export through the bacterial Sec pathway journal, November 2016

Structure of the substrate-engaged SecA-SecY protein translocation machine journal, June 2019

Preprotein mature domains contain translocase targeting signals that are essential for secretion journal, April 2017

The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria journal, April 2018

Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis journal, October 2018

Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2 journal, December 2015

Protein translocation by the SecA ATPase occurs by a power‐stroke mechanism journal, March 2019

The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity journal, June 2019

Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2 text, January 2016

Structure of the substrate-engaged SecA-SecY protein translocation machine journal, June 2019

Novel Sequence Feature of SecA Translocase Protein Unique to the Thermophilic Bacteria: Bioinformatics Analyses to Investigate Their Potential Roles journal, December 2019

Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
journal, November 2007

Mechanisms of Sec61/SecY-Mediated Protein Translocation Across Membranes
journal, June 2012

Protein Translocation Across the Bacterial Cytoplasmic Membrane
journal, June 2008

The Sec protein-translocation pathway
journal, October 2001

The Sec translocon mediated protein transport in prokaryotes and eukaryotes
journal, March 2014

BiP Acts as a Molecular Ratchet during Posttranslational Transport of Prepro-α Factor across the ER Membrane
journal, May 1999

SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
journal, September 1994

Structure and function of SecA, the preprotein translocase nanomotor
journal, November 2004

Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA
journal, September 2002

A large conformational change of the translocation ATPase SecA
journal, July 2004

A Novel Dimer Interface and Conformational Changes Revealed by an X-ray Structure of B. subtilis SecA
journal, December 2006

Structure of Dimeric SecA, the Escherichia coli Preprotein Translocase Motor
journal, March 2007

Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase
journal, February 2003

Crystal Structure of the Translocation ATPase SecA from Thermus thermophilus Reveals a Parallel, Head-to-Head Dimer
journal, December 2006

Conformational Flexibility and Peptide Interaction of the Translocation ATPase SecA
journal, December 2009

Structure of a complex of the ATPase SecA and the protein-translocation channel
journal, October 2008

A role for the two-helix finger of the SecA ATPase in protein translocation
journal, October 2008

A “Push and Slide” Mechanism Allows Sequence-Insensitive Translocation of Secretory Proteins by the SecA ATPase
journal, June 2014

ATPase Active-Site Electrostatic Interactions Control the Global Conformation of the 100 kDa SecA Translocase
journal, February 2013

Mapping polypeptide interactions of the SecA ATPase during translocation
journal, November 2009

A Recipe for the Computation of the Free Energy Barrier and the Lowest Free Energy Path of Concerted Reactions ^†
journal, April 2005

[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

Features and development of Coot
journal, March 2010

Towards automated crystallographic structure refinement with phenix.refine
journal, March 2012

Collaboration gets the most out of software
journal, September 2013

Optimization of the Additive CHARMM All-Atom Protein Force Field Targeting Improved Sampling of the Backbone ϕ, ψ and Side-Chain χ ₁ and χ ₂ Dihedral Angles
journal, August 2012

VMD: Visual molecular dynamics
journal, February 1996

Scalable molecular dynamics with NAMD
journal, January 2005

Calculating free energies using average force
journal, November 2001

Exploring Multidimensional Free Energy Landscapes Using Time-Dependent Biases on Collective Variables
journal, December 2009

Analysis of Polypeptide Movement in the SecY Channel during SecA-mediated Protein Translocation
journal, June 2008

X-Ray Diffraction data from Protein translocation ATPase SecA, source of 4YS0 structure
dataset, January 2015

X-Ray Diffraction data from Protein translocation ATPase SecA, source of 4YS0 structure
dataset, January 2015

Protein export through the bacterial Sec pathway
journal, November 2016

Structure of the substrate-engaged SecA-SecY protein translocation machine
journal, June 2019

Preprotein mature domains contain translocase targeting signals that are essential for secretion
journal, April 2017

The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria
journal, April 2018

Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis
journal, October 2018

Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2
journal, December 2015

Protein translocation by the SecA ATPase occurs by a power‐stroke mechanism
journal, March 2019

The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity
journal, June 2019

Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2
text, January 2016

Structure of the substrate-engaged SecA-SecY protein translocation machine
journal, June 2019

Novel Sequence Feature of SecA Translocase Protein Unique to the Thermophilic Bacteria: Bioinformatics Analyses to Investigate Their Potential Roles
journal, December 2019