1qu7

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[[Image:1qu7.jpg|left|200px]]
 
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{{Structure
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==FOUR HELICAL-BUNDLE STRUCTURE OF THE CYTOPLASMIC DOMAIN OF A SERINE CHEMOTAXIS RECEPTOR==
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|PDB= 1qu7 |SIZE=350|CAPTION= <scene name='initialview01'>1qu7</scene>, resolution 2.60&Aring;
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<StructureSection load='1qu7' size='340' side='right'caption='[[1qu7]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1qu7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QU7 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.6&#8491;</td></tr>
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|GENE=
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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=1qu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qu7 OCA], [https://pdbe.org/1qu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qu7 RCSB], [https://www.ebi.ac.uk/pdbsum/1qu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qu7 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qu7 OCA], [http://www.ebi.ac.uk/pdbsum/1qu7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qu7 RCSB]</span>
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[https://www.uniprot.org/uniprot/MCP1_ECOLI MCP1_ECOLI] Receptor for the attractant L-serine and related amino acids. Is also responsible for chemotaxis away from a wide range of repellents, including leucine, indole, and weak acids. Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.
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}}
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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/qu/1qu7_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/main_output.php?pdb_ID=1qu7 ConSurf].
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<div style="clear:both"></div>
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'''FOUR HELICAL-BUNDLE STRUCTURE OF THE CYTOPLASMIC DOMAIN OF A SERINE CHEMOTAXIS RECEPTOR'''
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==See Also==
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*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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*[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]]
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==Overview==
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__TOC__
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The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved. In contrast to many mammalian receptors which signal by oligomerizing upon ligand binding, the chemotaxis receptors are dimeric even in the absence of their ligands, and their signalling does not depend on a monomer-dimer equilibrium. Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors. Here we report the crystal structure of the cytoplasmic domain of a serine chemotaxis receptor of Escherichia coli, which reveals a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.
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</StructureSection>
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==About this Structure==
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1QU7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QU7 OCA].
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==Reference==
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Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10466731 10466731]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kim, K K.]]
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[[Category: Kim KK]]
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[[Category: Kim, S H.]]
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[[Category: Kim S-H]]
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[[Category: Yokota, H.]]
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[[Category: Yokota H]]
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[[Category: chemotaxis]]
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[[Category: four helical-bundle]]
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[[Category: serine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:19:05 2008''
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Current revision

FOUR HELICAL-BUNDLE STRUCTURE OF THE CYTOPLASMIC DOMAIN OF A SERINE CHEMOTAXIS RECEPTOR

PDB ID 1qu7

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