3c12

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[[Image:3c12.png|left|200px]]
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==Crystal Structure of FlgD from Xanthomonas campestris: Insights into the Hook Capping Essential for Flagellar Assembly==
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<StructureSection load='3c12' size='340' side='right' caption='[[3c12]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3c12]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C12 FirstGlance]. <br>
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</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=3c12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c12 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c12 RCSB], [http://www.ebi.ac.uk/pdbsum/3c12 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/3c12_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of the C-terminal domain of a hook-capping protein FlgD from the plant pathogen Xanthomonas campestris (Xc) has been determined to a resolution of ca 2.5 A using X-ray crystallography. The monomer of whole FlgD comprises 221 amino acids with a molecular mass of 22.7 kDa, but the flexible N-terminus is cleaved for up to 75 residues during crystallization. The final structure of the C-terminal domain reveals a novel hybrid comprising a tudor-like domain interdigitated with a fibronectin type III domain. The C-terminal domain of XcFlgD forms three types of dimers in the crystal. In agreement with this, analytical ultracentrifugation and gel filtration experiments reveal that they form a stable dimer in solution. From these results, we propose that the Xc flagellar hook cap protein FlgD comprises two individual domains, a flexible N-terminal domain that cannot be detected in the current study and a stable C-terminal domain that forms a stable dimer.
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{{STRUCTURE_3c12| PDB=3c12 | SCENE= }}
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Crystal structure of the C-terminal domain of a flagellar hook-capping protein from Xanthomonas campestris.,Kuo WT, Chin KH, Lo WT, Wang AH, Chou SH J Mol Biol. 2008 Aug 1;381(1):189-99. Epub 2008 Jun 7. PMID:18599076<ref>PMID:18599076</ref>
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===Crystal Structure of FlgD from Xanthomonas campestris: Insights into the Hook Capping Essential for Flagellar Assembly===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_18599076}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[3c12]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C12 OCA].
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</StructureSection>
[[Category: Xanthomonas campestris pv. campestris]]
[[Category: Xanthomonas campestris pv. campestris]]
[[Category: Chin, K H.]]
[[Category: Chin, K H.]]

Revision as of 21:10, 2 October 2014

Crystal Structure of FlgD from Xanthomonas campestris: Insights into the Hook Capping Essential for Flagellar Assembly

3c12, resolution 2.51Å

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