1F4V

CRYSTAL STRUCTURE OF ACTIVATED CHEY BOUND TO THE N-TERMINUS OF FLIM

1F4V の概要

• エントリーDOI: 10.2210/pdb1f4v/pdb
• 関連するPDBエントリー: 1DJM 1FQW 3CHY
• 分子名称: CHEMOTAXIS CHEY PROTEIN, FLAGELLAR MOTOR SWITCH PROTEIN, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: response regulator, peptide-protein complex, bacterial signal transduction, bef3, signaling protein
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell inner membrane; Peripheral membrane protein: P06974
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 47468.18

構造登録者

Lee, S.Y.,Cho, H.S.,Pelton, J.G.,Yan, D.,Henderson, R.K.,King, D.,Huang, L.S.,Kustu, S.,Berry, E.A.,Wemmer, D.E. (登録日: 2000-06-10, 公開日: 2001-01-17, 最終更新日: 2024-02-07)

主引用文献

Lee, S.Y.,Cho, H.S.,Pelton, J.G.,Yan, D.,Henderson, R.K.,King, D.S.,Huang, L.,Kustu, S.,Berry, E.A.,Wemmer, D.E.
Crystal structure of an activated response regulator bound to its target.
Nat.Struct.Biol., 8:52-56, 2001

PubMed Abstract: The chemotactic regulator CheY controls the direction of flagellar rotation in Escherichia coli. We have determined the crystal structure of BeF3--activated CheY from E. coli in complex with an N-terminal peptide derived from its target, FliM. The structure reveals that the first seven residues of the peptide pack against the beta4-H4 loop and helix H4 of CheY in an extended conformation, whereas residues 8-15 form two turns of helix and pack against the H4-beta5-H5 face. The peptide binds the only region of CheY that undergoes noticeable conformational change upon activation and would most likely be sandwiched between activated CheY and the remainder of FliM to reverse the direction of flagellar rotation.

PubMed: 11135671
DOI: 10.1038/83053

実験手法

X-RAY DIFFRACTION (2.22 Å)