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 |
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Main Authors: | , , , , , , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
5 Abbey Square, Chester, Cheshire CH1 2HU, England
Munksgaard International Publishers
01-04-2005
International Union of Crystallography |
Subjects: | |
Online Access: | Get full text |
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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). |
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Bibliography: | ark:/67375/WNG-MJTBV3FN-K istex:E51B42615C496AE2E6D9AD2B849DB615065DD72B ArticleID:AYF2EN5104 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1744-3091 1744-3091 |
DOI: | 10.1107/S1744309105007463 |