1jya
From Proteopedia
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'''Crystal Structure of SycE''' | '''Crystal Structure of SycE''' | ||
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[[Category: Birtalan, S.]] | [[Category: Birtalan, S.]] | ||
[[Category: Ghosh, P.]] | [[Category: Ghosh, P.]] | ||
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| - | [[Category: | + | [[Category: Type iii secretion]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:04:18 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:04, 2 May 2008
Crystal Structure of SycE
Overview
In the type III secretory system of bacterial pathogens, a large number of sequence-divergent but characteristically small (approximately 14-19 kDa), acidic (pI approximately 4-5) chaperone proteins have been identified. We present the 1.74 A resolution crystal structure of the Yersinia pseudotuberculosis chaperone SycE, whose action in promoting translocation of YopE into host macrophages is essential to Yersinia pathogenesis. SycE, a compact, globular dimer with a novel fold, has two large hydrophobic surface patches that may form binding sites for YopE or other type III components. These patches are formed by structurally key residues that are conserved among many chaperones, suggesting shared structural and functional relationships. A negative electrostatic potential covers almost the entire surface of SycE and is likely conserved in character, but not in detail, among chaperones. The structure provides the first structural insights into possible modes of action of SycE and type III chaperones in general.
About this Structure
1JYA is a Single protein structure of sequence from Yersinia pseudotuberculosis. Full crystallographic information is available from OCA.
Reference
Structure of the Yersinia type III secretory system chaperone SycE., Birtalan S, Ghosh P, Nat Struct Biol. 2001 Nov;8(11):974-8. PMID:11685245 Page seeded by OCA on Fri May 2 22:04:18 2008
