The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague |
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Authors: | Derewenda Urszula Mateja Agnieszka Devedjiev Yancho Routzahn Karen M Evdokimov Artem G Derewenda Zygmunt S Waugh David S |
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Institution: | Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA. |
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Abstract: | 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. |
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