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| | <StructureSection load='2ch4' size='340' side='right'caption='[[2ch4]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='2ch4' size='340' side='right'caption='[[2ch4]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ch4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CH4 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b3q|1b3q]], [[1i58|1i58]], [[1i59|1i59]], [[1i5a|1i5a]], [[1i5b|1i5b]], [[1i5c|1i5c]], [[1i5d|1i5d]], [[1tqg|1tqg]], [[1u0s|1u0s]], [[1k0s|1k0s]]</td></tr> | + | <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> |
| - | <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=2ch4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ch4 OCA], [http://pdbe.org/2ch4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ch4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ch4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ch4 ProSAT]</span></td></tr> | + | <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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CHEW_THEMA CHEW_THEMA]] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors (By similarity). | + | [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). |
| | == 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: Atcc 43589]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bilwes, A M]] | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Crane, B R]] | + | [[Category: Bilwes AM]] |
| - | [[Category: Park, S Y]] | + | [[Category: Crane BR]] |
| - | [[Category: Chemotaxis]] | + | [[Category: Park SY]] |
| - | [[Category: Histidine kinase]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Protein-protein complex]]
| + | |
| - | [[Category: Sensory transduction]]
| + | |
| - | [[Category: Signal transduction]]
| + | |
| - | [[Category: Transferase]]
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| - | [[Category: Transferase-chemotaxis complex]]
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| - | [[Category: Transferase/chemotaxis]]
| + | |
| Structural highlights
Function
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).
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
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Park SY, Borbat PP, Gonzalez-Bonet G, Bhatnagar J, Pollard AM, Freed JH, Bilwes AM, Crane BR. Reconstruction of the chemotaxis receptor-kinase assembly. Nat Struct Mol Biol. 2006 May;13(5):400-7. Epub 2006 Apr 23. PMID:16622408 doi:10.1038/nsmb1085
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