2CH7
Crystal structure of the cytoplasmic domain of a bacterial chemoreceptor from Thermotoga maritima
Summary for 2CH7
| Entry DOI | 10.2210/pdb2ch7/pdb |
| Descriptor | METHYL-ACCEPTING CHEMOTAXIS PROTEIN, LEAD (II) ION, ... (4 entities in total) |
| Functional Keywords | chemotaxis, receptor, four-helix bundle, signal transduction, methyl-accepting receptor |
| Biological source | THERMOTOGA MARITIMA More |
| Cellular location | Cell membrane; Multi-pass membrane protein (Potential): Q9X0M7 Q9X0M7 |
| Total number of polymer chains | 2 |
| Total formula weight | 67225.06 |
| Authors | Park, S.Y.,Bilwes, A.M.,Crane, B.R. (deposition date: 2006-03-13, release date: 2006-04-18, Last modification date: 2024-05-08) |
| Primary citation | Park, S.Y.,Borbat, P.P.,Gonzalez-Bonet, G.,Bhatnagar, J.,Pollard, A.M.,Freed, J.H.,Bilwes, A.M.,Crane, B.R. Reconstruction of the Chemotaxis Receptor-Kinase Assembly Nat.Struct.Mol.Biol., 13:400-, 2006 Cited by PubMed Abstract: 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. PubMed: 16622408DOI: 10.1038/NSMB1085 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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