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TitleHigh-syn conformation of uridine and asymmetry of the hexameric molecule revealed in the high-resolution structures of Shewanella oneidensis MR-1 uridine phosphorylase in the free form and in complex with uridine.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 70, Page 3310-3319, Year 2014
Publish dateAug 13, 2014 (structure data deposition date)
AuthorsSafonova, T.N. / Mikhailov, S.N. / Veiko, V.P. / Mordkovich, N.N. / Manuvera, V.A. / Alekseev, C.S. / Kovalchuk, M.V. / Popov, V.O. / Polyakov, K.M.
External linksActa Crystallogr. ,Sect. D / PubMed:25478848
MethodsX-ray diffraction
Resolution0.93 - 1.6 Å
Structure data

PDB-4r2w:
X-ray structure of uridine phosphorylase from Shewanella oneidensis MR-1 in complex with uridine at 1.6 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-4r2x:
Unique conformation of uridine and asymmetry of the hexameric molecule revealed in the high-resolution structures of Shewanella oneidensis uridine phosphorylase in the free form and in complex with uridine
Method: X-RAY DIFFRACTION / Resolution: 0.93 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-URI:
URIDINE

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

Source
  • shewanella oneidensis mr-1 (bacteria)
  • shewanella oneidensis (bacteria)
KeywordsTRANSFERASE / Uridine phosphorylase / Uridine Binding

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