1jya
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1jya" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jya, resolution 1.74Å" /> '''Crystal Structure of...)
Next diff →
Revision as of 16:33, 20 November 2007
|
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 Tue Nov 20 18:41:08 2007
