1r6f
From Proteopedia
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'''The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague''' | '''The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague''' | ||
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Revision as of 04:08, 3 May 2008
The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague
Overview
The LcrV protein (V-antigen) is a multifunctional virulence factor in Yersinia pestis, the causative agent of plague. LcrV regulates the translocation of cytotoxic effector proteins from the bacterium into the cytosol of mammalian cells via a type III secretion system, possesses antihost activities of its own, and is also an active and passive mediator of resistance to disease. Although a crystal structure of this protein has been actively sought for better understanding of its role in pathogenesis, the wild-type LcrV was found to be recalcitrant to crystallization. We employed a surface entropy reduction mutagenesis strategy to obtain crystals of LcrV that diffract to 2.2 A and determined its structure. The refined model reveals a dumbbell-like molecule with a novel fold that includes an unexpected coiled-coil motif, and provides a detailed three-dimensional roadmap for exploring structure-function relationships in this essential virulence determinant.
About this Structure
1R6F is a Single protein structure of sequence from Yersinia pestis. Full crystallographic information is available from OCA.
Reference
The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague., Derewenda U, Mateja A, Devedjiev Y, Routzahn KM, Evdokimov AG, Derewenda ZS, Waugh DS, Structure. 2004 Feb;12(2):301-6. PMID:14962390 Page seeded by OCA on Sat May 3 07:08:28 2008
