2hje

From Proteopedia

(Difference between revisions)

Revision as of 06:31, 27 June 2018

Crystal structure of Vibrio harveyi LuxQ periplasmic domain

Structural highlights

2hje is a 1 chain structure with sequence from "achromobacter_harveyi"_johnson_and_shunk_1936 "achromobacter harveyi" johnson and shunk 1936. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2hj9
Gene:	luxQ ("Achromobacter harveyi" Johnson and Shunk 1936)
Activity:	Histidine kinase, with EC number 2.7.13.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LUXQ_VIBHA] 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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Bacteria sense their environment using receptors of the histidine sensor kinase family, but how kinase activity is regulated by ligand binding is not well understood. Autoinducer-2 (AI-2), a secreted signaling molecule originally identified in studies of the marine bacterium Vibrio harveyi, regulates quorum-sensing responses and allows communication between different bacterial species. AI-2 signal transduction in V. harveyi requires the integral membrane receptor LuxPQ, comprised of periplasmic binding protein (LuxP) and histidine sensor kinase (LuxQ) subunits. Combined X-ray crystallographic and functional studies show that AI-2 binding causes a major conformational change within LuxP, which in turn stabilizes a quaternary arrangement in which two LuxPQ monomers are asymmetrically associated. We propose that formation of this asymmetric quaternary structure is responsible for repressing the kinase activity of both LuxQ subunits and triggering the transition of V. harveyi into quorum-sensing mode.

Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing.,Neiditch MB, Federle MJ, Pompeani AJ, Kelly RC, Swem DL, Jeffrey PD, Bassler BL, Hughson FM Cell. 2006 Sep 22;126(6):1095-108. PMID:16990134^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Neiditch MB, Federle MJ, Pompeani AJ, Kelly RC, Swem DL, Jeffrey PD, Bassler BL, Hughson FM. Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing. Cell. 2006 Sep 22;126(6):1095-108. PMID:16990134 doi:http://dx.doi.org/10.1016/j.cell.2006.07.032

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hje"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Vibrio harveyi LuxQ periplasmic domain==
 <StructureSection load='2hje' size='340' side='right' caption='[[2hje]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">luxQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=669 "Achromobacter harveyi" Johnson and Shunk 1936])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hje OCA], [http://pdbe.org/2hje PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hje RCSB], [http://www.ebi.ac.uk/pdbsum/2hje PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hje OCA], [http://pdbe.org/2hje PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hje RCSB], [http://www.ebi.ac.uk/pdbsum/2hje PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hje ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/2hje_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/2hje_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2hje

From Proteopedia

Revision as of 06:31, 27 June 2018

Crystal structure of Vibrio harveyi LuxQ periplasmic domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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