2hje

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[[Image:2hje.gif|left|200px]]
 
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{{Structure
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==Crystal structure of Vibrio harveyi LuxQ periplasmic domain==
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|PDB= 2hje |SIZE=350|CAPTION= <scene name='initialview01'>2hje</scene>, resolution 1.70&Aring;
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<StructureSection load='2hje' size='340' side='right'caption='[[2hje]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NI:NICKEL (II) ION'>NI</scene>
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<table><tr><td colspan='2'>[[2hje]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HJE FirstGlance]. <br>
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|ACTIVITY= [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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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|GENE= luxQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=669 Vibrio harveyi])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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}}
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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=2hje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hje OCA], [https://pdbe.org/2hje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hje RCSB], [https://www.ebi.ac.uk/pdbsum/2hje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hje ProSAT]</span></td></tr>
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</table>
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'''Crystal structure of Vibrio harveyi LuxQ periplasmic domain'''
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== Function ==
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[https://www.uniprot.org/uniprot/LUXQ_VIBHA 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.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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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.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/2hje_consurf.spt"</scriptWhenChecked>
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2HJE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJE OCA].
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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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==Reference==
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</jmolCheckbox>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16990134 16990134]
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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/main_output.php?pdb_ID=2hje ConSurf].
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[[Category: Histidine kinase]]
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<div style="clear:both"></div>
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[[Category: Single protein]]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Vibrio harveyi]]
[[Category: Vibrio harveyi]]
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[[Category: Hughson, F M.]]
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[[Category: Hughson FM]]
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[[Category: Kelly, R C.]]
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[[Category: Kelly RC]]
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[[Category: Neiditch, M B.]]
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[[Category: Neiditch MB]]
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[[Category: NI]]
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[[Category: autoinducer-2 (ai-2)]]
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[[Category: histidine sensor kinase]]
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[[Category: per/arnt/simple-minded (pas) fold]]
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[[Category: quorum sensing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:17:48 2008''
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Current revision

Crystal structure of Vibrio harveyi LuxQ periplasmic domain

PDB ID 2hje

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