3UT6
Crystal structure of E. Coli PNP complexed with PO4 and formycin A
Summary for 3UT6
| Entry DOI | 10.2210/pdb3ut6/pdb |
| Related | 3ONV 3OOE 3OOH 3OPV |
| Descriptor | Purine nucleoside phosphorylase deoD-type, (1S)-1-(7-amino-1H-pyrazolo[4,3-d]pyrimidin-3-yl)-1,4-anhydro-D-ribitol, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | purine nucleoside phosphorylase, formycin, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 3 |
| Total formula weight | 78441.48 |
| Authors | Stefanic, Z. (deposition date: 2011-11-25, release date: 2012-05-23, Last modification date: 2024-03-20) |
| Primary citation | Stefanic, Z.,Narczyk, M.,Mikleusevic, G.,Wielgus-Kutrowska, B.,Bzowska, A.,Luic, M. New phosphate binding sites in the crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with phosphate and formycin A. Febs Lett., 586:967-971, 2012 Cited by PubMed Abstract: 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. PubMed: 22569248DOI: 10.1016/j.febslet.2012.02.039 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.895 Å) |
Structure validation
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