3QDE
The structure of Cellobiose phosphorylase from Clostridium thermocellum in complex with phosphate
Summary for 3QDE
| Entry DOI | 10.2210/pdb3qde/pdb |
| Descriptor | Cellobiose phosphorylase, PHOSPHATE ION, TRIS-HYDROXYMETHYL-METHYL-AMMONIUM, ... (4 entities in total) |
| Functional Keywords | cellulase, cellobiose, phosphate, phosphorylase, transferase |
| Biological source | Clostridium thermocellum |
| Total number of polymer chains | 2 |
| Total formula weight | 186413.45 |
| Authors | Bianchetti, C.M.,Elsen, N.L.,Horn, M.K.,Fox, B.G.,Phillips Jr., G.N. (deposition date: 2011-01-18, release date: 2011-11-09, Last modification date: 2024-02-21) |
| Primary citation | Bianchetti, C.M.,Elsen, N.L.,Fox, B.G.,Phillips, G.N. Structure of cellobiose phosphorylase from Clostridium thermocellum in complex with phosphate. Acta Crystallogr.,Sect.F, 67:1345-1349, 2011 Cited by PubMed Abstract: 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 α-D-glucose 1-phosphate and D-glucose. CBP from C. thermocellum is a modular enzyme composed of four domains [N-terminal domain, helical linker, (α/α)(6)-barrel domain and C-terminal domain] and is a member of glycoside hydrolase family 94. The 2.4 Å 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. PubMed: 22102229DOI: 10.1107/S1744309111032660 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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