2ZLB

Crystal structure of APO form of rat catechol-O-methyltransferase

2ZLB の概要

• エントリーDOI: 10.2210/pdb2zlb/pdb
• 関連するPDBエントリー: 1VID
• 分子名称: Catechol O-methyltransferase, SULFATE ION (3 entities in total)
• 機能のキーワード: transferase, methyltransferase, neurotransmitter degradation, alternative initiation, catecholamine metabolism, cytoplasm, magnesium, membrane, metal-binding, phosphoprotein, s-adenosyl-l-methionine, signal-anchor, transmembrane, transferase (methyltransferase)
• 由来する生物種: Rattus norvegicus (Rat)
• 細胞内の位置: Isoform 2: Cytoplasm. Isoform 1: Cell membrane; Single-pass type II membrane protein; Extracellular side: P22734
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25012.59

構造登録者

Tsuji, E. (登録日: 2008-04-04, 公開日: 2008-10-07, 最終更新日: 2023-11-01)

主引用文献

Tsuji, E.,Okazaki, K.,Isaji, M.,Takeda, K.
Crystal structures of the Apo and Holo form of rat catechol-O-methyltransferase
J.Struct.Biol., 165:133-139, 2009

PubMed Abstract: Catechol-O-methyltransferase (COMT, EC 2.1.1.6) is a monomeric enzyme that catalyzes the transfer of a methyl group from S-adenosyl-l-methionine (AdoMet) to the phenolic oxygen of substituted catechols. Although the inhibitor recognition pattern and AdoMet site have already been studied crystallographically, structural information on the catalytic cycle of COMT has not yet been obtained. In this study, comparison of the co-factor and inhibitor-bound structures revealed that the Apo form of COMT shows a conformational change and there was no cleft corresponding to the AdoMet-binding site; the overall structure was partially open form and the substrate recognition site was not clearly defined. The Holo form of COMT was similar to the quaternary structure except for the beta6-beta7 and alpha2-alpha3 ligand recognition loops. These conformational changes provide a deeper insight into the structural events occurring in reactions catalyzed by AdoMet.

PubMed: 19111934
DOI: 10.1016/j.jsb.2008.11.012

実験手法

X-RAY DIFFRACTION (2.2 Å)