Article
Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Ce16A from trichoderma reesei.
Structure (London, England : 1993) - 15 Sept 1999
Zou J y, Kleywegt G J, Ståhlberg J, Driguez H, Nerinckx W, Claeyssens M, Koivula A, Teeri T T, Jones T A
Abstract excerpt
BACKGROUND: Cel6A is one of the two cellobiohydrolases produced by Trichoderma reesei. The catalytic core has a structure that is a variation of the classic TIM barrel. The active site is located inside a tunnel, the roof of which is formed mainly by a pair of loops. RESULTS: We describe three new ligand complexes. One is the structure of the wild-type enzyme in complex with a nonhydrolysable...
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