3ut6

Crystal structure of E. Coli PNP complexed with PO4 and formycin A

spinqualitylabelsall models 3ut6, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ut6 is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FMC, PO4 Related: 3onv, 3ooe, 3ooh, 3opv Activity: Purine-nucleoside phosphorylase, with EC number 2.4.2.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DEOD_ECOLI] Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules.[HAMAP-Rule:MF_01627] Publication Abstract from PubMed Purine nucleoside phosphorylase (PNP) from Escherichia coli is a homohexamer that catalyses the phosphorolytic cleavage of the glycosidic bond of purine nucleosides. The first crystal structure of the ternary complex of this enzyme (with a phosphate ion and formycin A), which is biased by neither the presence of an inhibitor nor sulfate as a precipitant, is presented. The structure reveals, in some active sites, an unexpected and never before observed binding site for phosphate and exhibits a stoichiometry of two phosphate molecules per enzyme subunit. Moreover, in these active sites, the phosphate and nucleoside molecules are found not to be in direct contact. Rather, they are bridged by three water molecules that occupy the "standard" phosphate binding site. New phosphate binding sites in the crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with phosphate and formycin A.,Stefanic Z, Narczyk M, Mikleusevic G, Wielgus-Kutrowska B, Bzowska A, Luic M FEBS Lett. 2012 Apr 5;586(7):967-71. Epub 2012 Mar 1. PMID:22569248 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Purine nucleoside phosphorylase

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