Structural highlights
Function
[UDP_ECOLI] Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Uridine phosphorylase from E. coli (Upase) has been crystallized using vapor diffusion technique in a new monoclinic crystal form. The structure was determined by the molecular replacement method at 2.5 A resolution. The coordinates of the trigonal crystal form were used as a starting model and the refinement by the program XPLOR led to the R-factor of 18.6%. The amino acid fold of the protein was found to be the same as that in the trigonal crystals. The positions of flexible regions were refined. The conclusion about the involvement in the active site is in good agreement with the results of the biochemical experiments.
Atomic structure at 2.5 A resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal lattice.,Morgunova EYu, Mikhailov AM, Popov AN, Blagova EV, Smirnova EA, Vainshtein BK, Mao C, Armstrong ShR, Ealick SE, Komissarov AA, et al. FEBS Lett. 1995 Jun 26;367(2):183-7. PMID:7796917[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Morgunova EYu, Mikhailov AM, Popov AN, Blagova EV, Smirnova EA, Vainshtein BK, Mao C, Armstrong ShR, Ealick SE, Komissarov AA, et al.. Atomic structure at 2.5 A resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal lattice. FEBS Lett. 1995 Jun 26;367(2):183-7. PMID:7796917
