7REQ

METHYLMALONYL-COA MUTASE, 2-CARBOXYPROPYL-COA INHIBITOR COMPLEX

7REQ の概要

• エントリーDOI: 10.2210/pdb7req/pdb
• 分子名称: PROTEIN (METHYLMALONYL-COA MUTASE), 2-CARBOXYPROPYL-COENZYME A, COBALAMIN, ... (6 entities in total)
• 機能のキーワード: isomerase, mutase, intramolecular transferase
• 由来する生物種: Propionibacterium freudenreichii subsp. shermanii; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 303872.41

構造登録者

Evans, P.R.,Mancia, F. (登録日: 1998-09-10, 公開日: 1998-09-16, 最終更新日: 2023-09-20)

主引用文献

Mancia, F.,Smith, G.A.,Evans, P.R.
Crystal structure of substrate complexes of methylmalonyl-CoA mutase.
Biochemistry, 38:7999-8005, 1999

PubMed Abstract: X-ray crystal structures of methylmalonyl-CoA mutase in complexes with substrate methylmalonyl-CoA and inhibitors 2-carboxypropyl-CoA and 3-carboxypropyl-CoA (substrate and product analogues) show that the enzyme-substrate interactions change little during the course of the rearrangement reaction, in contrast to the large conformational change on substrate binding. The substrate complex shows a 5'-deoxyadenine molecule in the active site, bound weakly and not attached to the cobalt atom of coenzyme B12, rotated and shifted from its position in the substrate-free adenosylcobalamin complex. The position of Tyralpha89 close to the substrate explains the stereochemical selectivity of the enzyme for (2R)-methylmalonyl-CoA.

PubMed: 10387043
DOI: 10.1021/bi9903852

実験手法

X-RAY DIFFRACTION (2.2 Å)