3seo

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[[Image:3seo.png|left|200px]]
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==Crystal structure of VopL C terminal domain==
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<StructureSection load='3seo' size='340' side='right' caption='[[3seo]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3seo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_parahaemolyticus Vibrio parahaemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SEO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SEO FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene><br>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VopL, VPA1370 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=670 Vibrio parahaemolyticus])</td></tr>
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<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=3seo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3seo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3seo RCSB], [http://www.ebi.ac.uk/pdbsum/3seo PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Vibrio parahaemolyticus protein L (VopL) is an actin nucleation factor that induces stress fibers when injected into eukaryotic host cells. VopL contains three N-terminal Wiskott-Aldrich homology 2 (WH2) motifs and a unique VopL C-terminal domain (VCD). We describe crystallographic and biochemical analyses of filament nucleation by VopL. The WH2 element of VopL does not nucleate on its own and requires the VCD for activity. The VCD forms a U-shaped dimer in the crystal, stabilized by a terminal coiled coil. Dimerization of the WH2 motifs contributes strongly to nucleation activity, as do contacts of the VCD to actin. Our data lead to a model in which VopL stabilizes primarily lateral (short-pitch) contacts between actin monomers to create the base of a two-stranded filament. Stabilization of lateral contacts may be a common feature of actin filament nucleation by WH2-based factors.
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Mechanism of actin filament nucleation by the bacterial effector VopL.,Yu B, Cheng HC, Brautigam CA, Tomchick DR, Rosen MK Nat Struct Mol Biol. 2011 Aug 28;18(9):1068-74. doi: 10.1038/nsmb.2110. PMID:21873984<ref>PMID:21873984</ref>
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The line below this paragraph, containing "STRUCTURE_3seo", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_3seo| PDB=3seo | SCENE= }}
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===Crystal structure of VopL C terminal domain===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_21873984}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 21873984 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_21873984}}
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==About this Structure==
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[[3seo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_parahaemolyticus Vibrio parahaemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SEO OCA].
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==Reference==
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<ref group="xtra">PMID:021873984</ref><references group="xtra"/>
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[[Category: Vibrio parahaemolyticus]]
[[Category: Vibrio parahaemolyticus]]
[[Category: Rosen, M K.]]
[[Category: Rosen, M K.]]

Revision as of 05:31, 5 June 2014

Crystal structure of VopL C terminal domain

3seo, resolution 2.31Å

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