Structural highlights
Publication Abstract from PubMed
Clostridium thermocellum is a cellulosome-producing bacterium that is able to efficiently degrade and utilize cellulose as a sole carbon source. Cellobiose phosphorylase (CBP) plays a critical role in cellulose degradation by catalyzing the reversible phosphate-dependent hydrolysis of cellobiose, the major product of cellulose degradation, into alpha-D-glucose 1-phosphate and D-glucose. CBP from C. thermocellum is a modular enzyme composed of four domains [N-terminal domain, helical linker, (alpha/alpha)(6)-barrel domain and C-terminal domain] and is a member of glycoside hydrolase family 94. The 2.4 A resolution X-ray crystal structure of C. thermocellum CBP reveals the residues involved in coordinating the catalytic phosphate as well as the residues that are likely to be involved in substrate binding and discrimination.
Structure of cellobiose phosphorylase from Clostridium thermocellum in complex with phosphate.,Bianchetti CM, Elsen NL, Fox BG, Phillips GN Jr Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt 11):1345-9., Epub 2011 Oct 25. PMID:22102229[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bianchetti CM, Elsen NL, Fox BG, Phillips GN Jr. Structure of cellobiose phosphorylase from Clostridium thermocellum in complex with phosphate. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt 11):1345-9., Epub 2011 Oct 25. PMID:22102229 doi:10.1107/S1744309111032660
