Literature summary for 2.4.1.266 extracted from

Albesa-Jove, D.; Romero-Garcia, J.; Sancho-Vaello, E.; Contreras, F.X.; Rodrigo-Unzueta, A.; Comino, N.; Carreras-Gonzalez, A.; Arrasate, P.; Urresti, S.; Biarnes, X.; Planas, A.; Guerin, M.E.
Structural snapshots and loop dynamics along the catalytic cycle of glycosyltransferase GpgS (2017), Structure, 25, 1034-1044 .

Search for more literature for 2.4.1.266

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of the unliganded form and in binary and ternary complexes with substrates. The L loop located in the active site adopts open and closed states. Both states coexist, but the conformational equilibrium is highly displaced to the open conformation. Both phosphoglycerate and UDP-Glc-Mn2+ can separately bind to the GpgS structure. Phosphoglycerate binds to a positively charged pocket located in the C-terminal domain of the enzyme, with the L loop displaying a closed conformation. UDP-Glc binds to a positively charged pocket mainly located in the N-terminal of the enzyme, with the alpha- and beta-phosphates coordinating the metal cofactor Mn2+. Following the reaction, glucosylphosphoglycerate is first released with the assistance of the highly disordered Loop 165-184	Mycobacterium tuberculosis

Crystallization (Comment)

Organism

structures of the unliganded form and in binary and ternary complexes with substrates. The L loop located in the active site adopts open and closed states. Both states coexist, but the conformational equilibrium is highly displaced to the open conformation. Both phosphoglycerate and UDP-Glc-Mn2+ can separately bind to the GpgS structure. Phosphoglycerate binds to a positively charged pocket located in the C-terminal domain of the enzyme, with the L loop displaying a closed conformation. UDP-Glc binds to a positively charged pocket mainly located in the N-terminal of the enzyme, with the alpha- and beta-phosphates coordinating the metal cofactor Mn2+. Following the reaction, glucosylphosphoglycerate is first released with the assistance of the highly disordered Loop 165-184

Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WMW9	-	-
Mycobacterium tuberculosis ATCC 25618	P9WMW9	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-glucose + 3-phospho-D-glycerate	-	Mycobacterium tuberculosis	UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate	-	?
UDP-glucose + 3-phospho-D-glycerate	-	Mycobacterium tuberculosis ATCC 25618	UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate	-	?

Synonyms

Synonyms	Comment	Organism
GpgS	-	Mycobacterium tuberculosis