3c30
From Proteopedia
(Difference between revisions)
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==Crystal structure of the Vibrio Cholerae LuxQ periplasmic domain (SeMet)== | ==Crystal structure of the Vibrio Cholerae LuxQ periplasmic domain (SeMet)== | ||
| - | <StructureSection load='3c30' size='340' side='right' caption='[[3c30]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='3c30' size='340' side='right'caption='[[3c30]], [[Resolution|resolution]] 2.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3c30]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3c30]] 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=3C30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C30 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3c38|3c38]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3c38|3c38]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">luxQ ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">luxQ ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 Vibrio cholerae])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c30 OCA], [https://pdbe.org/3c30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c30 RCSB], [https://www.ebi.ac.uk/pdbsum/3c30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c30 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: Large Structures]] | ||
[[Category: Vibrio cholerae]] | [[Category: Vibrio cholerae]] | ||
[[Category: Hendrickson, W]] | [[Category: Hendrickson, W]] | ||
Revision as of 07:41, 27 January 2022
Crystal structure of the Vibrio Cholerae LuxQ periplasmic domain (SeMet)
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