1QU7

FOUR HELICAL-BUNDLE STRUCTURE OF THE CYTOPLASMIC DOMAIN OF A SERINE CHEMOTAXIS RECEPTOR

1QU7 の概要

• エントリーDOI: 10.2210/pdb1qu7/pdb
• 分子名称: METHYL-ACCEPTING CHEMOTAXIS PROTEIN I (2 entities in total)
• 機能のキーワード: serine, chemotaxis, four helical-bundle, signaling protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane ; Multi- pass membrane protein : P02942
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47482.62

構造登録者

Kim, K.K.,Yokota, H.,Kim, S.-H. (登録日: 1999-07-07, 公開日: 2000-07-12, 最終更新日: 2024-02-14)

主引用文献

Kim, K.K.,Yokota, H.,Kim, S.H.
Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor.
Nature, 400:787-792, 1999

PubMed Abstract: The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved. In contrast to many mammalian receptors which signal by oligomerizing upon ligand binding, the chemotaxis receptors are dimeric even in the absence of their ligands, and their signalling does not depend on a monomer-dimer equilibrium. Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors. Here we report the crystal structure of the cytoplasmic domain of a serine chemotaxis receptor of Escherichia coli, which reveals a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.

PubMed: 10466731
DOI: 10.1038/23512

実験手法

X-RAY DIFFRACTION (2.6 Å)