5NZ8

Clostridium thermocellum cellodextrin phosphorylase with cellotetraose and phosphate bound

5NZ8 の概要

• エントリーDOI: 10.2210/pdb5nz8/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900011
• 分子名称: 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)
• 機能のキーワード: glycoside hydrolase family 94, cellodextrin phosphorylase, cellulose synthesis, hydrolase
• 由来する生物種: Clostridium thermocellum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 230518.36

構造登録者

O'Neill, E.C.,Pergolizzi, G.,Stevenson, C.E.M.,Lawson, D.M.,Nepogodiev, S.A.,Field, R.A. (登録日: 2017-05-12, 公開日: 2017-08-09, 最終更新日: 2024-01-17)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (3 Å)