1AF7

CHER FROM SALMONELLA TYPHIMURIUM

1AF7 の概要

• エントリーDOI: 10.2210/pdb1af7/pdb
• 分子名称: CHEMOTAXIS RECEPTOR METHYLTRANSFERASE CHER, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: methyltransferase, chemotaxis receptor methylation
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31917.45

構造登録者

Djordjevic, S.,Stock, A.M. (登録日: 1997-03-22, 公開日: 1998-01-28, 最終更新日: 2024-02-07)

主引用文献

Djordjevic, S.,Stock, A.M.
Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine.
Structure, 5:545-558, 1997

PubMed Abstract: Flagellated bacteria swim towards favorable chemicals and away from deleterious ones. The sensing of chemoeffector gradients involves chemotaxis receptors, transmembrane proteins that detect stimuli through their periplasmic domains and transduce signals via their cytoplasmic domains to the downstream signaling components. Signaling outputs from chemotaxis receptors are influenced both by the binding of the chemoeffector ligand to the periplasmic domain and by methylation of specific glutamate residues on the cytoplasmic domain of the receptor. Methylation is catalyzed by CheR, an S-adenosylmethionine-dependent methyltransferase. CheR forms a tight complex with the receptor by binding a region of the receptors that is distinct from the methylation site. CheR belongs to a broad class of enzymes involved in the methylation of a variety of substrates. Until now, no structure from the class of protein methyltransferases has been characterized.

PubMed: 9115443
DOI: 10.1016/S0969-2126(97)00210-4

実験手法

X-RAY DIFFRACTION (2 Å)