1l2w
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(New page: 200px<br /><applet load="1l2w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l2w, resolution 2.00Å" /> '''Crystal Structure of...)
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Revision as of 18:04, 20 November 2007
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Crystal Structure of the Yersinia Virulence Effector YopE Chaperone-binding Domain in Complex with its Secretion Chaperone, SycE
Overview
The type III secretion system (TTSS) of Gram-negative bacterial pathogens, delivers effector proteins required for virulence directly into the, cytosol of host cells. Delivery of many effectors depends on association, with specific cognate chaperones in the bacterial cytosol. The mechanism, of chaperone action is not understood. Here we present biochemical and, crystallographic results on the Yersinia SycE-YopE chaperone-effector, complex that contradict previous models of chaperone function and, demonstrate that chaperone action is isolated to only a small portion of, the effector. This, together with evidence for stereochemical conservation, between chaperone-effector complexes, which are otherwise unrelated in, sequence, indicates that these complexes function as general, three-dimensional TTSS secretion signals and may endow a temporal order to, secretion.
About this Structure
1L2W is a Single protein structure of sequence from Yersinia pseudotuberculosis. Full crystallographic information is available from OCA.
Reference
Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens., Birtalan SC, Phillips RM, Ghosh P, Mol Cell. 2002 May;9(5):971-80. PMID:12049734
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