1R6F

The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague

Summary for 1R6F

• Entry DOI: 10.2210/pdb1r6f/pdb
• Descriptor: Virulence-associated V antigen (1 entity in total)
• Functional Keywords: coiled-coil, protein binding
• Biological source: Yersinia pestis
• Cellular location: Secreted: P21206
• Total number of polymer chains: 1
• Total formula weight: 35158.56

Authors

Derewenda, U.,Mateja, A.,Devedjiev, Y.,Routzahn, K.M.,Evdokimov, A.G.,Derewenda, Z.S.,Waugh, D.S. (deposition date: 2003-10-15, release date: 2004-03-09, Last modification date: 2024-02-14)

Primary citation

Derewenda, U.,Mateja, A.,Devedjiev, Y.,Routzahn, K.M.,Evdokimov, A.G.,Derewenda, Z.S.,Waugh, D.S.
The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague
Structure, 12:301-306, 2004

PubMed 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.

PubMed: 14962390
DOI: 10.1016/j.str.2004.03.008

Experimental method

X-RAY DIFFRACTION (2.17 Å)