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| - | [[Image:2ibm.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2ibm| PDB=2ibm | SCENE= }} | | {{STRUCTURE_2ibm| PDB=2ibm | SCENE= }} |
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| - | '''A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA'''
| + | ===A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16989859}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16989859 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16989859}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Seca]] | | [[Category: Seca]] |
| | [[Category: Signal peptide binding]] | | [[Category: Signal peptide binding]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:17:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:30:31 2008'' |
Revision as of 03:30, 29 July 2008
Template:STRUCTURE 2ibm
A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA
Template:ABSTRACT PUBMED 16989859
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
Page seeded by OCA on Tue Jul 29 06:30:31 2008
