5TC9

Wild type TrCel7A catalytic domain in a closed state

Summary for 5TC9

Entry DOI	10.2210/pdb5tc9/pdb
Descriptor	Glucanase, 2-acetamido-2-deoxy-beta-D-glucopyranose, GADOLINIUM ION, ... (5 entities in total)
Functional Keywords	cel7a, cbhi, cellulase, hydrolase
Biological source	Hypocrea jecorina (strain QM6a)
Total number of polymer chains	1
Total formula weight	46749.45
Authors	Bodenheimer, A.M.,Meilleur, F. (deposition date: 2016-09-14, release date: 2017-01-04, Last modification date: 2024-10-30)
Primary citation	Bodenheimer, A.M.,Meilleur, F. Crystal structures of wild-type Trichoderma reesei Cel7A catalytic domain in open and closed states. FEBS Lett., 590:4429-4438, 2016 Cited by PubMed Abstract: Trichoderma reesei Cel7A efficiently hydrolyses cellulose. We report here the crystallographic structures of the wild-type TrCel7A catalytic domain (CD) in an open state and, for the first time, in a closed state. Molecular dynamics (MD) simulations indicate that the loops along the CD tunnel move in concerted motions. Together, the crystallographic and MD data suggest that the CD cycles between the tense and relaxed forms that are characteristic of work producing enzymes. Analysis of the interactions formed by R251 provides a structural rationale for the concurrent decrease in product inhibition and catalytic efficiency measured for product-binding site mutants. PubMed: 27943301 DOI: 10.1002/1873-3468.12464 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.6 Å)

Structure validation