2ch4

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[[Image:2ch4.gif|left|200px]]
 
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{{Structure
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==Complex between Bacterial Chemotaxis histidine kinase CheA domains P4 and P5 and receptor-adaptor protein CheW==
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|PDB= 2ch4 |SIZE=350|CAPTION= <scene name='initialview01'>2ch4</scene>, resolution 3.5&Aring;
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<StructureSection load='2ch4' size='340' side='right'caption='[[2ch4]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Anp+Binding+Site+For+Chain+B'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>
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<table><tr><td colspan='2'>[[2ch4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CH4 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]] 3.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr>
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|DOMAIN=
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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=2ch4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ch4 OCA], [https://pdbe.org/2ch4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ch4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ch4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ch4 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ch4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ch4 OCA], [http://www.ebi.ac.uk/pdbsum/2ch4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ch4 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/CHEA_THEMA CHEA_THEMA] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY (By similarity).
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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/ch/2ch4_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=2ch4 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In bacterial chemotaxis, an assembly of transmembrane receptors, the CheA histidine kinase and the adaptor protein CheW processes environmental stimuli to regulate motility. The structure of a Thermotoga maritima receptor cytoplasmic domain defines CheA interaction regions and metal ion-coordinating charge centers that undergo chemical modification to tune receptor response. Dimeric CheA-CheW, defined by crystallography and pulsed ESR, positions two CheWs to form a cleft that is lined with residues important for receptor interactions and sized to clamp one receptor dimer. CheW residues involved in kinase activation map to interfaces that orient the CheW clamps. CheA regulatory domains associate in crystals through conserved hydrophobic surfaces. Such CheA self-contacts align the CheW receptor clamps for binding receptor tips. Linking layers of ternary complexes with close-packed receptors generates a lattice with reasonable component ratios, cooperative interactions among receptors and accessible sites for modification enzymes.
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'''COMPLEX BETWEEN BACTERIAL CHEMOTAXIS HISTIDINE KINASE CHEA DOMAINS P4 AND P5 AND RECEPTOR-ADAPTOR PROTEIN CHEW'''
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Reconstruction of the chemotaxis receptor-kinase assembly.,Park SY, Borbat PP, Gonzalez-Bonet G, Bhatnagar J, Pollard AM, Freed JH, Bilwes AM, Crane BR Nat Struct Mol Biol. 2006 May;13(5):400-7. Epub 2006 Apr 23. PMID:16622408<ref>PMID:16622408</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ch4" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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In bacterial chemotaxis, an assembly of transmembrane receptors, the CheA histidine kinase and the adaptor protein CheW processes environmental stimuli to regulate motility. The structure of a Thermotoga maritima receptor cytoplasmic domain defines CheA interaction regions and metal ion-coordinating charge centers that undergo chemical modification to tune receptor response. Dimeric CheA-CheW, defined by crystallography and pulsed ESR, positions two CheWs to form a cleft that is lined with residues important for receptor interactions and sized to clamp one receptor dimer. CheW residues involved in kinase activation map to interfaces that orient the CheW clamps. CheA regulatory domains associate in crystals through conserved hydrophobic surfaces. Such CheA self-contacts align the CheW receptor clamps for binding receptor tips. Linking layers of ternary complexes with close-packed receptors generates a lattice with reasonable component ratios, cooperative interactions among receptors and accessible sites for modification enzymes.
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*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
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*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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==About this Structure==
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== References ==
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2CH4 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CH4 OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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Reconstruction of the chemotaxis receptor-kinase assembly., Park SY, Borbat PP, Gonzalez-Bonet G, Bhatnagar J, Pollard AM, Freed JH, Bilwes AM, Crane BR, Nat Struct Mol Biol. 2006 May;13(5):400-7. Epub 2006 Apr 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16622408 16622408]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Bilwes, A M.]]
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[[Category: Bilwes AM]]
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[[Category: Crane, B R.]]
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[[Category: Crane BR]]
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[[Category: Park, S Y.]]
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[[Category: Park SY]]
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[[Category: chemotaxis]]
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[[Category: histidine kinase]]
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[[Category: phosphorylation]]
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[[Category: protein-protein complex]]
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[[Category: sensory transduction]]
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[[Category: signal transduction]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:21:24 2008''
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Current revision

Complex between Bacterial Chemotaxis histidine kinase CheA domains P4 and P5 and receptor-adaptor protein CheW

PDB ID 2ch4

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