2Q0Q

Structure of the Native M. Smegmatis Aryl Esterase

2Q0Q の概要

• エントリーDOI: 10.2210/pdb2q0q/pdb
• 関連するPDBエントリー: 2q0s
• 分子名称: aryl esterase, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: sgnh hydrolase, oligomeric enzyme, acyl transfer, aryl esterase, hydrolase
• 由来する生物種: Mycobacterium smegmatis
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 189554.78

構造登録者

Mathews, I.I.,Soltis, M.,Saldajeno, M.,Ganshaw, G.,Sala, R.,Weyler, W.,Cervin, M.A.,Whited, G.,Bott, R. (登録日: 2007-05-22, 公開日: 2007-12-11, 最終更新日: 2011-07-13)

主引用文献

Mathews, I.,Soltis, M.,Saldajeno, M.,Ganshaw, G.,Sala, R.,Weyler, W.,Cervin, M.A.,Whited, G.,Bott, R.
Structure of a novel enzyme that catalyzes acyl transfer to alcohols in aqueous conditions.
Biochemistry, 46:8969-8979, 2007

PubMed Abstract: The unusual architecture of the enzyme (MsAcT) isolated from Mycobacterium smegmatis forms the mechanistic basis for favoring alcoholysis over hydrolysis in water. Unlike hydrolases that perform alcoholysis only under anhydrous conditions, MsAcT demonstrates alcoholysis in substantially aqueous media and, in the presence of hydrogen peroxide, has a perhydrolysis:hydrolysis ratio 50-fold greater than that of the best lipase tested. The crystal structures of the apoenzyme and an inhibitor-bound form have been determined to 1.5 A resolution. MsAcT is an octamer in the asymmetric unit and forms a tightly associated aggregate in solution. Relative to other structurally similar monomers, MsAcT contains several insertions that contribute to the oligomerization and greatly restrict the shape of the active site, thereby limiting its accessibility. These properties create an environment by which MsAcT can catalyze transesterification reactions in an aqueous medium and suggests how a serine hydrolase can be engineered to be an efficient acyltransferase.

PubMed: 17636869
DOI: 10.1021/bi7002444

実験手法

X-RAY DIFFRACTION (1.5 Å)