2CH7

Crystal structure of the cytoplasmic domain of a bacterial chemoreceptor from Thermotoga maritima

2CH7 の概要

• エントリーDOI: 10.2210/pdb2ch7/pdb
• 分子名称: METHYL-ACCEPTING CHEMOTAXIS PROTEIN, LEAD (II) ION, ... (4 entities in total)
• 機能のキーワード: chemotaxis, receptor, four-helix bundle, signal transduction, methyl-accepting receptor
• 由来する生物種: THERMOTOGA MARITIMA; 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein (Potential): Q9X0M7 Q9X0M7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67225.06

構造登録者

Park, S.Y.,Bilwes, A.M.,Crane, B.R. (登録日: 2006-03-13, 公開日: 2006-04-18, 最終更新日: 2024-05-08)

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 (2.5 Å)