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5O59

Cellobiohydrolase Cel7A from T. atroviride

Summary for 5O59
Entry DOI10.2210/pdb5o59/pdb
DescriptorGlucanase, 2-acetamido-2-deoxy-beta-D-glucopyranose, NICKEL (II) ION, ... (9 entities in total)
Functional Keywordshydrolase, glycoside hydrolase, cellobiohydrolase, cellulase
Biological sourceHypocrea atroviridis
Total number of polymer chains2
Total formula weight94397.08
Authors
Borisova, A.S.,Stahlberg, J.,Hansson, H. (deposition date: 2017-06-01, release date: 2018-01-31, Last modification date: 2024-10-23)
Primary citationBorisova, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

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