3GBS

Crystal structure of Aspergillus oryzae cutinase

3GBS の概要

• エントリーDOI: 10.2210/pdb3gbs/pdb
• 分子名称: Cutinase 1 (2 entities in total)
• 機能のキーワード: serine esterase, alpha beta hydrolase, hydrolase, secreted
• 由来する生物種: Aspergillus oryzae
• 細胞内の位置: Secreted: P52956
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20636.34

構造登録者

Gosser, Y.,Lu, Z.,Alemu, G.,Li, H.,Kong, X.,Liu, Z.,Montclare, J. (登録日: 2009-02-20, 公開日: 2009-10-06, 最終更新日: 2024-11-20)

主引用文献

Liu, Z.,Gosser, Y.,Baker, P.J.,Ravee, Y.,Lu, Z.,Alemu, G.,Li, H.,Butterfoss, G.L.,Kong, X.P.,Gross, R.,Montclare, J.K.
Structural and functional studies of Aspergillus oryzae cutinase: enhanced thermostability and hydrolytic activity of synthetic ester and polyester degradation.
J.Am.Chem.Soc., 131:15711-15716, 2009

PubMed Abstract: Cutinases are responsible for hydrolysis of the protective cutin lipid polyester matrix in plants and thus have been exploited for hydrolysis of small molecule esters and polyesters. Here we explore the reactivity, stability, and structure of Aspergillus oryzae cutinase and compare it to the well-studied enzyme from Fusarium solani. Two critical differences are highlighted in the crystallographic analysis of the A. oryzae structure: (i) an additional disulfide bond and (ii) a topologically favored catalytic triad with a continuous and deep groove. These structural features of A. oryzae cutinase are proposed to result in an improved hydrolytic activity and altered substrate specificity profile, enhanced thermostability, and remarkable reactivity toward the degradation of the synthetic polyester polycaprolactone. The results presented here provide insight into engineering new cutinase-inspired biocatalysts with tailor-made properties.

PubMed: 19810726
DOI: 10.1021/ja9046697

実験手法

X-RAY DIFFRACTION (1.75 Å)