5NZ8
Clostridium thermocellum cellodextrin phosphorylase with cellotetraose and phosphate bound
Summary for 5NZ8
Entry DOI | 10.2210/pdb5nz8/pdb |
Related PRD ID | PRD_900011 |
Descriptor | Cellodextrin phosphorylase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, PHOSPHATE ION (3 entities in total) |
Functional Keywords | glycoside hydrolase family 94, cellodextrin phosphorylase, cellulose synthesis, hydrolase |
Biological source | Clostridium thermocellum |
Total number of polymer chains | 2 |
Total formula weight | 230518.36 |
Authors | O'Neill, E.C.,Pergolizzi, G.,Stevenson, C.E.M.,Lawson, D.M.,Nepogodiev, S.A.,Field, R.A. (deposition date: 2017-05-12, release date: 2017-08-09, Last modification date: 2024-01-17) |
Primary citation | O'Neill, E.C.,Pergolizzi, G.,Stevenson, C.E.M.,Lawson, D.M.,Nepogodiev, S.A.,Field, R.A. Cellodextrin phosphorylase from Ruminiclostridium thermocellum: X-ray crystal structure and substrate specificity analysis. Carbohydr. Res., 451:118-132, 2017 Cited by PubMed Abstract: The GH94 glycoside hydrolase cellodextrin phosphorylase (CDP, EC 2.4.1.49) produces cellodextrin oligomers from short β-1→4-glucans and α-D-glucose 1-phosphate. Compared to cellobiose phosphorylase (CBP), which produces cellobiose from glucose and α-D-glucose 1-phosphate, CDP is biochemically less well characterised. Herein, we investigate the donor and acceptor substrate specificity of recombinant CDP from Ruminiclostridium thermocellum and we isolate and characterise a glucosamine addition product to the cellobiose acceptor with the non-natural donor α-D-glucosamine 1-phosphate. In addition, we report the first X-ray crystal structure of CDP, along with comparison to the available structures from CBPs and other closely related enzymes, which contributes to understanding of the key structural features necessary to discriminate between monosaccharide (CBP) and oligosaccharide (CDP) acceptor substrates. PubMed: 28760417DOI: 10.1016/j.carres.2017.07.005 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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