Comparison of Crystal Structures of 10 Wrought Heat Resisting Alloys at Elevated Temperatures with Their Crystal Structures at Room Temperatures
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Manuscript to submit to Review of Scientific Instruments.
Trichoderma reesei Cel7A efficiently hydrolyses cellulose. We report here the crystallographic structures of the wild‐type Tr Cel7A 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.
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