1r6f: Difference between revisions

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<StructureSection load='1r6f' size='340' side='right'caption='[[1r6f]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
<StructureSection load='1r6f' size='340' side='right'caption='[[1r6f]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1r6f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1R6F FirstGlance]. <br>
<table><tr><td colspan='2'>[[1r6f]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1R6F FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r6f OCA], [https://pdbe.org/1r6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r6f RCSB], [https://www.ebi.ac.uk/pdbsum/1r6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r6f ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.17&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r6f OCA], [https://pdbe.org/1r6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r6f RCSB], [https://www.ebi.ac.uk/pdbsum/1r6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r6f ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/LCRV_YERPE LCRV_YERPE]] Possibly involved in calcium regulation of YOP expression, which includes the export process.  
[https://www.uniprot.org/uniprot/LCRV_YERPE LCRV_YERPE] Possibly involved in calcium regulation of YOP expression, which includes the export process.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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/main_output.php?pdb_ID=1r6f ConSurf].
</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/main_output.php?pdb_ID=1r6f ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 1r6f" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Derewenda, U]]
[[Category: Yersinia pestis]]
[[Category: Derewenda, Z S]]
[[Category: Derewenda U]]
[[Category: Devedjiev, Y]]
[[Category: Derewenda ZS]]
[[Category: Evdokimov, A G]]
[[Category: Devedjiev Y]]
[[Category: Mateja, A]]
[[Category: Evdokimov AG]]
[[Category: Routzahn, K M]]
[[Category: Mateja A]]
[[Category: Waugh, D S]]
[[Category: Routzahn KM]]
[[Category: Coiled-coil]]
[[Category: Waugh DS]]
[[Category: Protein binding]]

Latest revision as of 08:20, 14 February 2024

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

1r6f, resolution 2.17Å

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