4CSI

Crystal structure of the thermostable Cellobiohydrolase Cel7A from the fungus Humicola grisea var. thermoidea.

4CSI の概要

• エントリーDOI: 10.2210/pdb4csi/pdb
• 分子名称: CELLULASE, 2-acetamido-2-deoxy-beta-D-glucopyranose, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: hydrolase, glycoside hydrolase
• 由来する生物種: HUMICOLA GRISEA VAR. THERMOIDEA
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94882.53

構造登録者

Haddad-Momeni, M.,Goedegebuur, F.,Hansson, H.,Karkehabadi, S.,Askarieh, G.,Mitchinson, C.,Larenas, E.,Stahlberg, J.,Sandgren, M. (登録日: 2014-03-07, 公開日: 2014-09-10, 最終更新日: 2024-10-09)

主引用文献

Haddad-Momeni, M.,Goedegebuur, F.,Hansson, H.,Karkehabadi, S.,Askarieh, G.,Mitchinson, C.,Larenas, E.,Stahlberg, J.,Sandgren, M.
Expression, Crystal Structure and Cellulase Activity of the Thermostable Cellobiohydrolase Cel7A from the Fungus Humicola Grisea Var. Thermoidea.
Acta Crystallogr.,Sect.D, 70:2356-, 2014

PubMed Abstract: Glycoside hydrolase family 7 (GH7) cellobiohydrolases (CBHs) play a key role in biomass recycling in nature. They are typically the most abundant enzymes expressed by potent cellulolytic fungi, and are also responsible for the majority of hydrolytic potential in enzyme cocktails for industrial processing of plant biomass. The thermostability of the enzyme is an important parameter for industrial utilization. In this study, Cel7 enzymes from different fungi were expressed in a fungal host and assayed for thermostability, including Hypocrea jecorina Cel7A as a reference. The most stable of the homologues, Humicola grisea var. thermoidea Cel7A, exhibits a 10°C higher melting temperature (T(m) of 72.5°C) and showed a 4-5 times higher initial hydrolysis rate than H. jecorina Cel7A on phosphoric acid-swollen cellulose and showed the best performance of the tested enzymes on pretreated corn stover at elevated temperature (65°C, 24 h). The enzyme shares 57% sequence identity with H. jecorina Cel7A and consists of a GH7 catalytic module connected by a linker to a C-terminal CBM1 carbohydrate-binding module. The crystal structure of the H. grisea var. thermoidea Cel7A catalytic module (1.8 Å resolution; R(work) and R(free) of 0.16 and 0.21, respectively) is similar to those of other GH7 CBHs. The deviations of several loops along the cellulose-binding path between the two molecules in the asymmetric unit indicate higher flexibility than in the less thermostable H. jecorina Cel7A.

PubMed: 25195749
DOI: 10.1107/S1399004714013844

実験手法

X-RAY DIFFRACTION (1.8 Å)