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5NZ8

Clostridium thermocellum cellodextrin phosphorylase with cellotetraose and phosphate bound

Summary for 5NZ8
Entry DOI10.2210/pdb5nz8/pdb
Related PRD IDPRD_900011
DescriptorCellodextrin 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 Keywordsglycoside hydrolase family 94, cellodextrin phosphorylase, cellulose synthesis, hydrolase
Biological sourceClostridium thermocellum
Total number of polymer chains2
Total formula weight230518.36
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 citationO'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: 28760417
DOI: 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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