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1l2w

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

Structural highlights

1l2w is a 12 chain structure with sequence from Yersinia pseudotuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A0N9NJF3_YERPU Positive regulator of YopE.[PIRNR:PIRNR011271]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Birtalan SC, Phillips RM, Ghosh P. Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens. Mol Cell. 2002 May;9(5):971-80. PMID:12049734