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1r6f
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(New page: 200px<br /><applet load="1r6f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r6f, resolution 2.17Å" /> '''The structure of Yer...)
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Revision as of 23:11, 20 November 2007
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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 Wed Nov 21 01:18:27 2007
