5O5D

Cellobiohydrolase Cel7A from T. atroviride

Summary for 5O5D

• Entry DOI: 10.2210/pdb5o5d/pdb
• Descriptor: Glucanase, 2-acetamido-2-deoxy-beta-D-glucopyranose, NICKEL (II) ION, ... (8 entities in total)
• Functional Keywords: hydrolase, glycoside hydrolase, cellobiohydrolase, cellulase
• Biological source: Hypocrea atroviridis (strain ATCC 20476 / IMI 206040)
• Total number of polymer chains: 2
• Total formula weight: 92943.26

Authors

Borisova, A.S.,Stahlberg, J.,Hansson, H. (deposition date: 2017-06-01, release date: 2018-01-31, Last modification date: 2024-11-06)

Primary citation

Borisova, A.S.,Eneyskaya, E.V.,Jana, S.,Badino, S.F.,Kari, J.,Amore, A.,Karlsson, M.,Hansson, H.,Sandgren, M.,Himmel, M.E.,Westh, P.,Payne, C.M.,Kulminskaya, A.A.,Stahlberg, J.
Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from Trichoderma atroviride, T. reesei and T. harzianum.
Biotechnol Biofuels, 11:5-5, 2018

PubMed Abstract: The ascomycete fungus is the predominant source of enzymes for industrial conversion of lignocellulose. Its glycoside hydrolase family 7 cellobiohydrolase (GH7 CBH) Cel7A constitutes nearly half of the enzyme cocktail by weight and is the major workhorse in the cellulose hydrolysis process. The orthologs from (Cel7A) and (Cel7A) show high sequence identity with Cel7A, ~ 80%, and represent naturally evolved combinations of cellulose-binding tunnel-enclosing loop motifs, which have been suggested to influence intrinsic cellobiohydrolase properties, such as endo-initiation, processivity, and off-rate.

PubMed: 29344086
DOI: 10.1186/s13068-017-1006-7

Experimental method

X-RAY DIFFRACTION (1.72 Å)