1lx7

Structure of E. coli uridine phosphorylase at 2.0AStructure of E. coli uridine phosphorylase at 2.0A

Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN 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 The 2.0 A crystal structure has been determined for Escherichia coli uridine phosphorylase (UP), an essential enzyme in nucleotide biosynthesis that catalyzes the phosphorolytic cleavage of the C-N glycosidic bond of uridine to ribose-1-phosphate and uracil. The structure determination of two independent monomers in the asymmetric unit revealed the residue composition and atomic details of the apo configurations of each active site. The native hexameric UP enzyme was revealed by applying threefold crystallographic symmetry to the contents of the asymmetric unit. The 2.0 A model reveals a closer structural relationship to other nucleotide phosphorylase enzymes than was previously appreciated. Structure of Escherichia coli uridine phosphorylase at 2.0 A.,Burling FT, Kniewel R, Buglino JA, Chadha T, Beckwith A, Lima CD Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):73-6. Epub 2002 Dec, 19. PMID:12499542 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Uridine phosphorylase 3D structures

spinqualitylabelsall models 1lx7, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image