1jya
From Proteopedia
(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...) |
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| - | [[Image:1jya.gif|left|200px]]<br /><applet load="1jya" size=" | + | [[Image:1jya.gif|left|200px]]<br /><applet load="1jya" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jya, resolution 1.74Å" /> | caption="1jya, resolution 1.74Å" /> | ||
'''Crystal Structure of SycE'''<br /> | '''Crystal Structure of SycE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In the type III secretory system of bacterial pathogens, a large number of | + | 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== | ==About this Structure== | ||
| - | 1JYA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis]. Full crystallographic information is available from [http:// | + | 1JYA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JYA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: type iii secretion]] | [[Category: type iii secretion]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:03 2008'' |
Revision as of 11:28, 21 February 2008
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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 Thu Feb 21 13:28:03 2008
