2CH4
Complex between Bacterial Chemotaxis histidine kinase CheA domains P4 and P5 and receptor-adaptor protein CheW
Summary for 2CH4
| Entry DOI | 10.2210/pdb2ch4/pdb |
| Related | 1B3Q 1I58 1I59 1I5A 1I5B 1I5C 1I5D 1K0S 1TQG 1U0S |
| Descriptor | CHEMOTAXIS PROTEIN CHEA, CHEMOTAXIS PROTEIN CHEW, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | transferase/chemotaxis, chemotaxis, protein-protein complex, signal transduction, histidine kinase, sensory transduction, phosphorylation, transferase, transferase-chemotaxis complex |
| Biological source | THERMOTOGA MARITIMA More |
| Cellular location | Cytoplasm (Potential): Q56310 Cytoplasm (By similarity): Q56311 |
| Total number of polymer chains | 4 |
| Total formula weight | 106070.31 |
| Authors | Park, S.Y.,Bilwes, A.M.,Crane, B.R. (deposition date: 2006-03-10, release date: 2006-04-18, Last modification date: 2023-12-13) |
| 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 (3.5 Å) |
Structure validation
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