1GPI

Cellobiohydrolase Cel7D (CBH 58) from Phanerochaete chrysosporium. Catalytic module at 1.32 Angstrom resolution

1GPI の概要

• エントリーDOI: 10.2210/pdb1gpi/pdb
• 分子名称: EXOGLUCANASE I, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: hydrolase, glycosidase, cellulase, beta-glucanase, glycoprotein, cellulose degradation, enzyme, reaction center, extracellular, exoglucanase
• 由来する生物種: PHANEROCHAETE CHRYSOSPORIUM
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45998.35

構造登録者

Munoz, I.G.,Mowbray, S.L.,Stahlberg, J. (登録日: 2001-11-05, 公開日: 2002-01-01, 最終更新日: 2024-11-13)

主引用文献

Munoz, I.G.,Ubhayasekera, W.,Henriksson, H.,Szabo, I.,Pettersson, G.,Johansson, G.,Mowbray, S.L.,Stahlberg, J.
Family 7 Cellobiohydrolases from Phanerochaete Chrysosporium: Crystal Structure of the Catalytic Module of Cel7D (Cbh58) at 1.32 Angstrom Resolution and Homology Models of the Isozymes.
J.Mol.Biol., 314:1097-, 2001

PubMed Abstract: Cellobiohydrolase 58 (Cel7D) is the major cellulase produced by the white-rot fungus Phanerochaete chrysosporium, constituting approximately 10 % of the total secreted protein in liquid culture on cellulose. The enzyme is classified into family 7 of the glycosyl hydrolases, together with cellobiohydrolase I (Cel7A) and endoglucanase I (Cel7B) from Trichoderma reesei. Like those enzymes, it catalyses cellulose hydrolysis with net retention of the anomeric carbon configuration. The structure of the catalytic module (431 residues) of Cel7D was determined at 3.0 A resolution using the structure of Cel7A from T. reesei as a search model in molecular replacement, and ultimately refined at 1.32 A resolution. The core structure is a beta-sandwich composed of two large and mainly antiparallel beta-sheets packed onto each other. A long cellulose-binding groove is formed by loops on one face of the sandwich. The catalytic residues are conserved and the mechanism is expected to be the same as for other family members. The Phanerochaete Cel7D binding site is more open than that of the T. reesei cellobiohydrolase, as a result of deletions and other changes in the loop regions, which may explain observed differences in catalytic properties. The binding site is not, however, as open as the groove of the corresponding endoglucanase. A tyrosine residue at the entrance of the tunnel may be part of an additional subsite not present in the T. reesei cellobiohydrolase. The Cel7D structure was used to model the products of the five other family 7 genes found in P. chrysosporium. The results suggest that at least two of these will have differences in specificity and possibly catalytic mechanism, thus offering some explanation for the presence of Cel7 isozymes in this species, which are differentially expressed in response to various growth conditions.

PubMed: 11743726
DOI: 10.1006/JMBI.2000.5180

実験手法

X-RAY DIFFRACTION (1.32 Å)