Open AccessPreliminary investigation of the three‐dimensional structure of Salmonella typhimurium uridine phosphorylase in the crystalline state
Author(s) -
Molchan Olga K.,
Zhang Yang,
Dontsova Maria V.,
Lashkov Alexandr A.,
Garber Maria B.,
Gabdoulkhakov Azat G.,
Mironov Alexandr S.,
Morgunova Ekaterina Yu.,
Zhukhlistova Nadegda E.,
Voelter Wolfgang,
Betzel Christian,
Ealick Steven E.,
Mikhailov Al'bert M.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105007463
Subject(s) - glycosidic bond , uridine , nucleotide salvage , monomer , chemistry , ribose , uracil , stereochemistry , escherichia coli , pyrimidine , phosphorolysis , crystallography , hydrogen bond , active site , glycogen phosphorylase , thymidine phosphorylase , nucleotide , rna , molecule , enzyme , biochemistry , purine nucleoside phosphorylase , dna , organic chemistry , purine , gene , polymer
Uridine phosphorylase (UPh) catalyzes the phosphorolytic cleavage of the C—N glycosidic bond of uridine to ribose 1‐phosphate and uracil in the pyrimidine‐salvage pathway. The crystal structure of the Salmonella typhimurium uridine phosphorylase (StUPh) has been determined at 2.5 Å resolution and refined to an R factor of 22.1% and an R free of 27.9%. The hexameric StUPh displays 32 point‐group symmetry and utilizes both twofold and threefold non‐crystallographic axes. A phosphate is bound at the active site and forms hydrogen bonds to Arg91, Arg30, Thr94 and Gly26 of one monomer and Arg48 of an adjacent monomer. The hexameric StUPh model reveals a close structural relationship to Escherichia coli uridine phosphorylase (EcUPh).