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

Zimmer J, Li W, Rapoport TA
J Mol Biol 364 259-65 (2006)
Cited: 64 times
EuropePMC logo PMID: 16989859

Abstract

The SecA ATPase moves polypeptides post-translationally across the plasma membrane of eubacteria, but the mechanism of transport is still unclear. We describe the crystal structure of a novel dimeric form of Bacillus subtilis SecA. Dimerization of SecA occurs at the prominent groove formed by the nucleotide binding domain 2 (nbd2) and the preprotein cross-linking (ppx) domain. The dimer interface is very large, burying approximately 5400 A(2) of solvent accessible surface per monomer. Single cysteine disulfide cross-linking shows the presence of this novel SecA dimer in solution. In addition, other dimers also exist in solution, arguing that they all are in equilibrium with monomeric SecA and supporting the idea that the monomer may be the functional species. Dimerization of SecA causes an alpha-helix of one subunit to convert to a short beta-strand that participates in beta-sheet formation with strands in the other subunit. This conversion of secondary structure elements occurs close to the connection between the nbd1 and ppx domains, a potential site of interaction with translocation substrate. Comparing the different X-ray structures of B. subtilis SecA suggests that small changes in the nucleotide binding domains could be amplified via helix 1 of the helical scaffold domain (hsd) to generate larger movements of the domains involved in polypeptide binding.

Reviews - 2ibm mentioned but not cited (2)

  1. The Sec System: Protein Export in Escherichia coli. Crane JM, Randall LL. EcoSal Plus 7 (2017)
  2. SecA: a potential antimicrobial target. Chaudhary AS, Chen W, Jin J, Tai PC, Wang B. Future Med Chem 7 989-1007 (2015)

Articles - 2ibm mentioned but not cited (9)



Reviews citing this publication (22)

  1. Protein translocation across the bacterial cytoplasmic membrane. Driessen AJ, Nouwen N. Annu Rev Biochem 77 643-667 (2008)
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  9. SecA: a tale of two protomers. Sardis MF, Economou A. Mol Microbiol 76 1070-1081 (2010)
  10. Pushing, pulling and trapping--modes of motor protein supported protein translocation. Tomkiewicz D, Nouwen N, Driessen AJ. FEBS Lett 581 2820-2828 (2007)
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  12. The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria. Cranford-Smith T, Huber D. FEMS Microbiol Lett 365 fny093 (2018)
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  17. Protein Transport Across the Bacterial Plasma Membrane by the Sec Pathway. Smets D, Loos MS, Karamanou S, Economou A. Protein J 38 262-273 (2019)
  18. Use of synthetic signal sequences to explore the protein export machinery. Clérico EM, Maki JL, Gierasch LM. Biopolymers 90 307-319 (2008)
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  20. Single-Molecule Studies on the Protein Translocon. Seinen AB, Driessen AJM. Annu Rev Biophys 48 185-207 (2019)
  21. Bacterial Signal Peptides- Navigating the Journey of Proteins. Kaushik S, He H, Dalbey RE. Front Physiol 13 933153 (2022)
  22. Dynamic hydrogen-bond networks in bacterial protein secretion. Karathanou K, Bondar AN. FEMS Microbiol Lett 365 (2018)

Articles citing this publication (31)



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