Preliminary investigation of the three-dimensional structure of Salmonella typhimurium uridine phosphorylase in the crystalline state

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 r...

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Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 61; no. 4; pp. 337 - 340
Main Authors: 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.
Format: Journal Article
Language:English
Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01-04-2005
International Union of Crystallography
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Summary: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 Rfree 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).
Bibliography:ark:/67375/WNG-MJTBV3FN-K
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ArticleID:AYF2EN5104
ObjectType-Article-1
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ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309105007463