3c38
From Proteopedia
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<StructureSection load='3c38' size='340' side='right'caption='[[3c38]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3c38' size='340' side='right'caption='[[3c38]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3c38]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3c38]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C38 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c38 OCA], [https://pdbe.org/3c38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c38 RCSB], [https://www.ebi.ac.uk/pdbsum/3c38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c38 ProSAT]</span></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=3c38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c38 OCA], [https://pdbe.org/3c38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c38 RCSB], [https://www.ebi.ac.uk/pdbsum/3c38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c38 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/LUXQ_VIBCH LUXQ_VIBCH] At low cell density, in absence of AI-2 (autoinducer 2), LuxQ has a kinase activity and autophosphorylates on a histidine residue. The phosphoryl group is then transferred to an aspartate residue in the response regulator domain. The phosphoryl group is transferred to LuxU, and ultimately to LuxO. At high cell density, in the presence of AI-2, the kinase activity is inactivated, and the response regulator domain has a phosphatase activity (By similarity). | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Bacillo virgola del koch trevisan 1884]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Vibrio cholerae]] |
| - | [[Category: | + | [[Category: Hendrickson W]] |
| - | [[Category: | + | [[Category: Slama B]] |
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Current revision
Crystal structure of the periplasmic domain of Vibrio Cholerae LuxQ
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