1r6f
From Proteopedia
(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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| - | [[Image:1r6f.jpg|left|200px]]<br /><applet load="1r6f" size=" | + | [[Image:1r6f.jpg|left|200px]]<br /><applet load="1r6f" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r6f, resolution 2.17Å" /> | caption="1r6f, resolution 2.17Å" /> | ||
'''The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague'''<br /> | '''The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The LcrV protein (V-antigen) is a multifunctional virulence factor in | + | 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== | ==About this Structure== | ||
| - | 1R6F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http:// | + | 1R6F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R6F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Yersinia pestis]] | [[Category: Yersinia pestis]] | ||
[[Category: Derewenda, U.]] | [[Category: Derewenda, U.]] | ||
| - | [[Category: Derewenda, Z | + | [[Category: Derewenda, Z S.]] |
[[Category: Devedjiev, Y.]] | [[Category: Devedjiev, Y.]] | ||
| - | [[Category: Evdokimov, A | + | [[Category: Evdokimov, A G.]] |
[[Category: Mateja, A.]] | [[Category: Mateja, A.]] | ||
| - | [[Category: Routzahn, K | + | [[Category: Routzahn, K M.]] |
| - | [[Category: Waugh, D | + | [[Category: Waugh, D S.]] |
[[Category: coiled-coil]] | [[Category: coiled-coil]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:35 2008'' |
Revision as of 12:47, 21 February 2008
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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
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