1L2W

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

Summary for 1L2W

• Entry DOI: 10.2210/pdb1l2w/pdb
• Descriptor: YopE regulator, Outer membrane virulence protein yopE (3 entities in total)
• Functional Keywords: chaperone and virulence protein, chaperone
• Biological source: Yersinia pseudotuberculosis; More
• Cellular location: Cell outer membrane: 1L2W
• Total number of polymer chains: 12
• Total formula weight: 139860.66

Authors

Birtalan, S.C.,Phillips, R.M.,Ghosh, P. (deposition date: 2002-02-25, release date: 2002-06-12, Last modification date: 2023-08-16)

Primary citation

Birtalan, S.C.,Phillips, R.M.,Ghosh, P.
Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens.
Mol.Cell, 9:971-980, 2002

PubMed Abstract: 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.

PubMed: 12049734
DOI: 10.1016/S1097-2765(02)00529-4

Experimental method

X-RAY DIFFRACTION (2 Å)