1l2w
From Proteopedia
(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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| - | [[Image:1l2w.gif|left|200px]]<br /><applet load="1l2w" size=" | + | [[Image:1l2w.gif|left|200px]]<br /><applet load="1l2w" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l2w, resolution 2.00Å" /> | caption="1l2w, resolution 2.00Å" /> | ||
'''Crystal Structure of the Yersinia Virulence Effector YopE Chaperone-binding Domain in Complex with its Secretion Chaperone, SycE'''<br /> | '''Crystal Structure of the Yersinia Virulence Effector YopE Chaperone-binding Domain in Complex with its Secretion Chaperone, SycE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The type III secretion system (TTSS) of Gram-negative bacterial pathogens | + | 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== | ==About this Structure== | ||
| - | 1L2W 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:// | + | 1L2W 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=1L2W OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Yersinia pseudotuberculosis]] | [[Category: Yersinia pseudotuberculosis]] | ||
| - | [[Category: Birtalan, S | + | [[Category: Birtalan, S C.]] |
[[Category: Ghosh, P.]] | [[Category: Ghosh, P.]] | ||
| - | [[Category: Phillips, R | + | [[Category: Phillips, R M.]] |
[[Category: chaperone and virulence protein]] | [[Category: chaperone and virulence protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:42 2008'' |
Revision as of 11:40, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 13:40:42 2008
