Literature summary for 2.4.2.3 extracted from

Lashkov, A.; Zhukhlistova, N.; Sotnichenko, S.; Gabdulkhakov, A.; Mikhailov, A.
Structural basis for the mechanism of inhibition of uridine phosphorylase from Salmonella typhimurium (2010), Crystallogr. Rep., 55, 41-57.

No PubMed abstract available

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Salmonella enterica subsp. enterica serovar Typhimurium

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with with the inhibitor 2,2'-anhydrouridine, the substrate phosphate, and with both the inhibitor 2,2'-anhydrouridine and the substrate phosphate, to 2.38, 1.5 and 1.75 A resolution, respectively. The presence of the phosphate ion in the phosphate-binding site substantially changes the orientations of the side chains of the amino-acid residues Arg30, Arg91, and Arg48 coordinated to this ion. The highly flexible loop L9 is unstable	Salmonella enterica subsp. enterica serovar Typhimurium

Crystallization (Comment)

Organism

in complex with with the inhibitor 2,2'-anhydrouridine, the substrate phosphate, and with both the inhibitor 2,2'-anhydrouridine and the substrate phosphate, to 2.38, 1.5 and 1.75 A resolution, respectively. The presence of the phosphate ion in the phosphate-binding site substantially changes the orientations of the side chains of the amino-acid residues Arg30, Arg91, and Arg48 coordinated to this ion. The highly flexible loop L9 is unstable

Salmonella enterica subsp. enterica serovar Typhimurium

Organism

Organism	UniProt	Comment	Textmining
Salmonella enterica subsp. enterica serovar Typhimurium	P0A1F6	-	-

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Release 2023.1 (January 2023)