2ibm
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= secA, div+ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= secA, div+ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1m6n|1M6N]], [[1tf2|1TF2]], [[1nkt|1NKT]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ibm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ibm OCA], [http://www.ebi.ac.uk/pdbsum/2ibm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ibm RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Rapoport, T A.]] | [[Category: Rapoport, T A.]] | ||
[[Category: Zimmer, J.]] | [[Category: Zimmer, J.]] | ||
| - | [[Category: ADP]] | ||
[[Category: protein translocation]] | [[Category: protein translocation]] | ||
[[Category: seca]] | [[Category: seca]] | ||
[[Category: signal peptide binding]] | [[Category: signal peptide binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:42:05 2008'' |
Revision as of 00:42, 31 March 2008
| |||||||
| , resolution 3.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | secA, div+ (Bacillus subtilis) | ||||||
| Related: | 1M6N, 1TF2, 1NKT
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA
Overview
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.
About this Structure
2IBM is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
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. 2006 Dec 1;364(3):259-65. Epub 2006 Aug 22. PMID:16989859
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