1r6f

<StructureSection load='1r6f' size='340' side='right' caption='[[1r6f]], [[Resolution|resolution]] 2.17&Aring;' scene=''>

<table><tr><td colspan='2'>[[1r6f]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R6F FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1r6f RCSB], [http://www.ebi.ac.uk/pdbsum/1r6f PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r6/1r6f_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:14962390</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Derewenda, U.]]

[[Category: Derewenda, Z S.]]

[[Category: Devedjiev, Y.]]

[[Category: Evdokimov, A G.]]

[[Category: Mateja, A.]]

[[Category: Routzahn, K M.]]

[[Category: Waugh, D S.]]

[[Category: Protein binding]]