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PDBsum entry 1r6f
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Protein binding
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PDB id
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1r6f
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The structure of yersinia pestis V-Antigen, An essential virulence factor and mediator of immunity against plague.
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Authors
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U.Derewenda,
A.Mateja,
Y.Devedjiev,
K.M.Routzahn,
A.G.Evdokimov,
Z.S.Derewenda,
D.S.Waugh.
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Ref.
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Structure, 2004,
12,
301-306.
[DOI no: ]
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PubMed id
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Abstract
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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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Figure 3.
Figure 3. Front and Back Views of the Surface of LcrVAmino
acid residues that are conserved in P. aeruginosa PcrV are
colored brown.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
301-306)
copyright 2004.
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