1pr2 | pdb_00001pr2

Escherichia coli Purine Nucleoside Phosphorylase Complexed with 9-beta-D-[2-deoxyribofuranosyl]-6-methylpurine and Phosphate/Sulfate

spinqualitylabelsall models 1pr2, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pr2 is a 3 chain structure with sequence from Escherichia coli o157:h7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MDR, PO4 Related: 1ecp, 1k9s, 1pk7, 1pr0, 1pr1, 1pr4, 1pr5, 1pr6 Activity: Purine-nucleoside phosphorylase, with EC number 2.4.2.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DEOD_ECO57] Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. 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 Purine nucleoside phosphorylase catalyzes reversible phosphorolysis of purine nucleosides and 2'-deoxypurine nucleosides to the free base and ribose (or 2'-deoxyribose) 1-phosphate. Whereas the human enzyme is specific for 6-oxopurine ribonucleosides, the Escherichia coli enzyme accepts additional substrates including 6-oxopurine ribonucleosides, 6-aminopurine ribonucleosides, and to a lesser extent purine arabinosides. These differences have been exploited in a potential suicide gene therapy treatment for solid tumors. In an effort to optimize this suicide gene therapy approach, we have determined the three-dimensional structure of the E. coli enzyme in complex with 10 nucleoside analogs and correlated the structures with kinetic measurements and computer modeling. These studies explain the preference of the enzyme for ribose sugars, show increased flexibility for active site residues Asp204 and Arg24, and suggest that interactions involving the 1- and 6-positions of the purine and the 4'- and 5'-positions of the ribose provide the best opportunities to increase prodrug specificity and enzyme efficiency. Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase.,Bennett EM, Li C, Allan PW, Parker WB, Ealick SE J Biol Chem. 2003 Nov 21;278(47):47110-8. Epub 2003 Aug 21. PMID:12937174 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Purine nucleoside phosphorylase 3D structures

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