2CH4

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

2CH4 の概要

• エントリーDOI: 10.2210/pdb2ch4/pdb
• 関連するPDBエントリー: 1B3Q 1I58 1I59 1I5A 1I5B 1I5C 1I5D 1K0S 1TQG 1U0S
• 分子名称: CHEMOTAXIS PROTEIN CHEA, CHEMOTAXIS PROTEIN CHEW, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: transferase/chemotaxis, chemotaxis, protein-protein complex, signal transduction, histidine kinase, sensory transduction, phosphorylation, transferase, transferase-chemotaxis complex
• 由来する生物種: THERMOTOGA MARITIMA; 詳細
• 細胞内の位置: Cytoplasm (Potential): Q56310; Cytoplasm (By similarity): Q56311
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 106070.31

構造登録者

Park, S.Y.,Bilwes, A.M.,Crane, B.R. (登録日: 2006-03-10, 公開日: 2006-04-18, 最終更新日: 2023-12-13)

主引用文献

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

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: 16622408
DOI: 10.1038/NSMB1085

実験手法

X-RAY DIFFRACTION (3.5 Å)