1C4W

1.9 A STRUCTURE OF A-THIOPHOSPHONATE MODIFIED CHEY D57C

1C4W の概要

• エントリーDOI: 10.2210/pdb1c4w/pdb
• 関連するPDBエントリー: 3CHY
• 分子名称: CHEMOTAXIS PROTEIN CHEY (2 entities in total)
• 機能のキーワード: phosphono-chey, active form of the response regulator, chemotaxis, signaling 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: 14063.20

構造登録者

Halkides, C.J.,McEvoy, M.M.,Matsumura, P.,Volz, K.,Dahlquist, F.W. (登録日: 1999-09-28, 公開日: 2000-05-08, 最終更新日: 2023-12-27)

主引用文献

Halkides, C.J.,McEvoy, M.M.,Casper, E.,Matsumura, P.,Volz, K.,Dahlquist, F.W.
The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY.
Biochemistry, 39:5280-5286, 2000

PubMed Abstract: To structurally characterize the activated state of the transiently phosphorylated signal transduction protein CheY, we have constructed an alpha-thiophosphonate derivative of the CheY D57C point mutant and determined its three-dimensional structure at 1.85 A resolution. We have also characterized this analogue with high-resolution NMR and studied its binding to a peptide derived from FliM, CheY's target component of the flagellar motor. The chemically modified derivative, phosphono-CheY, exhibits many of the chemical properties of phosphorylated wild-type CheY, except that it is indefinitely stable. Electron density for the alpha-thiophosphonate substitution is clear and readily interpretable; omit refinement density at the phosphorus atom is greater than 10sigma. The molecule shows a number of localized conformational changes that are believed to constitute the postphosphorylation activation events. The most obvious of these changes include movement of the side chain of the active site base, Lys 109, and a predominately buried conformation of the side chain of Tyr 106. In addition, there are a number of more subtle changes more distant from the active site involving the alpha4 and alpha5 helices. These results are consistent with our previous structural interpretations of other CheY activation mutants, and with our earlier hypotheses concerning CheY activation through propagation of structural changes away from the active site.

PubMed: 10819997
DOI: 10.1021/bi9925524

実験手法

X-RAY DIFFRACTION (1.84 Å)