Crystal structures of wild-type Trichoderma reesei Cel7A catalytic domain in open and closed states

Journal Article · Mon Nov 07 00:00:00 EST 2016 · FEBS Letters

DOI:https://doi.org/10.1002/1873-3468.12464· OSTI ID:1338981

Bodenheimer, Annette M. ^[1]; Meilleur, Flora ^[1]

---

1. Molecular and Structural Biochemistry Department, North Carolina State University, Raleigh NC USA; Neutron Sciences Directorate, Oak Ridge National Laboratory, TN USA

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.

• Research Organization: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
• Sponsoring Organization: USDOE; National Science Foundation (NSF)
• OSTI ID: 1338981
• Journal Information: FEBS Letters, Vol. 590, Issue 23; ISSN 0014-5793
• Publisher: Federation of European Biochemical Societies
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES