1CHN

MAGNESIUM BINDING TO THE BACTERIAL CHEMOTAXIS PROTEIN CHEY RESULTS IN LARGE CONFORMATIONAL CHANGES INVOLVING ITS FUNCTIONAL SURFACE

1CHN の概要

• エントリーDOI: 10.2210/pdb1chn/pdb
• 分子名称: CHEY, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: signal transduction protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14005.44

構造登録者

Bellsolell, L.,Coll, M. (登録日: 1994-04-20, 公開日: 1994-07-31, 最終更新日: 2024-02-07)

主引用文献

Bellsolell, L.,Prieto, J.,Serrano, L.,Coll, M.
Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface.
J.Mol.Biol., 238:489-495, 1994

PubMed Abstract: The three-dimensional crystal structure of the bacterial chemotaxis protein CheY with the essential Mg2+ cation bound to the active site reveals large conformational changes caused by the metal binding. Displacements of up to 10 A are observed in several residues at the N terminus of alpha-helix 4 and in the preceding loop. One turn of this helix unwinds, and an Asn residue that was located inside the helix becomes the new N-cap. This supports the important role that N or C-cap residues play in alpha-helix stability. In addition the preceding beta-strand becomes elongated and a new beta-turn appears. The final effect is a significant modification of the surface relief of the protein in a region previously indicated, by genetic analysis, to be essential for CheY function. It is suggested that binding of a divalent cation to CheY could play a significant part in CheY activation and consequently in signal transduction in prokaryotes.

PubMed: 8176739
DOI: 10.1006/jmbi.1994.1308

実験手法

X-RAY DIFFRACTION (1.76 Å)