Literature summary for 2.4.1.20 extracted from

Bianchetti, C.; Elsen, N.; Fox, B.; Phillips, G.
Structure of cellobiose phosphorylase from Clostridium thermocellum in complex with phosphate (2011), Acta Crystallogr. Sect. F, 67, 1345-1349.

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with phosphate, to 2.4 A resolution. Enzyme is composed of four distinct domains, an N-terminal domain with residues 1-279, a helical linker with residues 280-314, an (alpha/beta)6-barrel domain with residues 321-734, and a C-terminal beta-sandwich domain with residues 315-320 and 735-811. The side chains of His653, Gln699 and Thr718 and the backbone N-atom of Gly719 coordinate the phosphate bound in the interior of the (alpha/beta)6-barrel domain. Two short helical extensions, residues 158-169, from the N-terminal domain of the adjacent subunit extend into the cleft which runs along the face of the (alpha/beta)6-barrel domain, forming an active-site pocket. An additional loop, residues 488-507, lays on top of the active-site pocket, forming a restrictive active-site pocket that is large enough to bind a disaccharide but not large enough to bind an oligosaccharide	Acetivibrio thermocellus

Crystallization (Comment)

Organism

in complex with phosphate, to 2.4 A resolution. Enzyme is composed of four distinct domains, an N-terminal domain with residues 1-279, a helical linker with residues 280-314, an (alpha/beta)6-barrel domain with residues 321-734, and a C-terminal beta-sandwich domain with residues 315-320 and 735-811. The side chains of His653, Gln699 and Thr718 and the backbone N-atom of Gly719 coordinate the phosphate bound in the interior of the (alpha/beta)6-barrel domain. Two short helical extensions, residues 158-169, from the N-terminal domain of the adjacent subunit extend into the cleft which runs along the face of the (alpha/beta)6-barrel domain, forming an active-site pocket. An additional loop, residues 488-507, lays on top of the active-site pocket, forming a restrictive active-site pocket that is large enough to bind a disaccharide but not large enough to bind an oligosaccharide

Acetivibrio thermocellus

Organism

Organism	UniProt	Comment	Textmining
Acetivibrio thermocellus	Q8VP44	member of glycoside hydrolase family 94	-

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Release 2023.1 (January 2023)