1l2w: Difference between revisions

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~~'''~~Crystal Structure of the Yersinia Virulence Effector YopE Chaperone-binding Domain in Complex with its Secretion Chaperone, SycE~~'''~~

===Crystal Structure of the Yersinia Virulence Effector YopE Chaperone-binding Domain in Complex with its Secretion Chaperone, SycE===

~~==Overview==~~

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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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12049734}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12049734 is the PubMed ID number.

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==About this Structure==

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[[Category: Phillips, R M.]]

[[Category: Chaperone and virulence protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 23:28:45 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:34:47 2008''

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-[[Image:1l2w.gif|left|200px]]
+{{Seed}}
+[[Image:1l2w.png|left|200px]]
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 {{STRUCTURE_1l2w|  PDB=1l2w  |  SCENE=  }}
-'''Crystal Structure of the Yersinia Virulence Effector YopE Chaperone-binding Domain in Complex with its Secretion Chaperone, SycE'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12049734}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12049734 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12049734}}
 ==About this Structure==
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 [[Category: Phillips, R M.]]
 [[Category: Chaperone and virulence protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:28:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 11:34:47 2008''