ATPase Active-Site Electrostatic Interactions Control the Global Conformation of the 100 kDa SecA Translocase (Q27675185)

4

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author name string

Dorothy M Kim

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Haiyan Zheng

2

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Yuanpeng J Huang

3

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John F Hunt

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language of work or name

English

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publication date

27 February 2013

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number of pages

12

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Journal of the American Chemical Society

inferred from page(s)

published in

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volume

135

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issue

8

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page(s)

2999-3010

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cites work

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2 June 2018

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2 June 2018

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2 June 2018

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Carboxy-terminal region of Escherichia coli SecA ATPase is important to promote its protein translocation activity in vivo.

2 June 2018

1 reference

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2 June 2018

1 reference

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27 November 2018

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Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state

27 November 2018

1 reference

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Global co-ordination of protein translocation by the SecA IRA1 switch

27 November 2018

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27 November 2018

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27 November 2018

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Lipid and signal peptide-induced conformational changes within the C-domain of Escherichia coli SecA protein

27 November 2018

1 reference

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27 November 2018

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Domain interactions of the peripheral preprotein Translocase subunit SecA.

27 November 2018

1 reference

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SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF.

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4134686

SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4134686

Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding

27 November 2018

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12 December 2020

Reconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE, and SecG (p12)

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12 December 2020

Thermodynamic parameters from hydrogen exchange measurements

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Interaction between SecA and SecYEG in Micellar Solution and Formation of the Membrane-Inserted State†

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Thermodynamics of nucleotide binding to NBS-I of the Bacillus subtilis preprotein translocase subunit SecA

1 reference

12 December 2020

Disorder breathes life into a DEAD motor

1 reference

12 December 2020

Nucleotide binding activity of SecA homodimer is conformationally regulated by temperature and altered by prlD and azi mutations

1 reference

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A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA

1 reference

12 December 2020