3LBF

Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli

3LBF の概要

• エントリーDOI: 10.2210/pdb3lbf/pdb
• 分子名称: Protein-L-isoaspartate O-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: modified rossman-type fold, methyltransferase, s-adenosyl-l-methionine, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A7A5
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 96143.45

構造登録者

Fang, P.,Li, X.,Wang, J.,Niu, L.,Teng, M. (登録日: 2010-01-08, 公開日: 2010-09-08, 最終更新日: 2023-11-01)

主引用文献

Fang, P.,Li, X.,Wang, J.,Xing, L.,Gao, Y.,Niu, L.,Teng, M.
Crystal structure of the protein L-isoaspartyl methyltransferase from Escherichia coli
Cell Biochem.Biophys., 58:163-167, 2010

PubMed Abstract: Among the known covalent damages that can occur spontaneously to proteins, the formation of isoaspartyl linkages through deamidation of asparagines and isomerization of aspartates may be one of the most rapid forms under conditions of physiological pH and temperature. The protein L-isoaspartyl methyltransferase (PIMT) is thought to recognize L-isoaspartyl residues and repair this kind of damaged proteins. Curiously, there is a potential functional difference between bacterial and mammalian PIMTs. Herein, we present the crystal structure of Escherichia coli PIMT (EcPIMT) at a resolution of 1.8 Å. The enzyme we investigated was able to remain bound to its product S-adenosylhomocysteine (SAH) during crystallization. Analysis indicates that the high affinity of EcPIMT for SAH might lead to the lower activity of the enzyme.

PubMed: 20857228
DOI: 10.1007/s12013-010-9103-2

実験手法

X-RAY DIFFRACTION (1.8 Å)