1ECP
PURINE NUCLEOSIDE PHOSPHORYLASE
Summary for 1ECP
| Entry DOI | 10.2210/pdb1ecp/pdb |
| Descriptor | PURINE NUCLEOSIDE PHOSPHORYLASE (2 entities in total) |
| Functional Keywords | pentosyltransferase, purine nucleoside phosphorylase, glycosyltransferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 6 |
| Total formula weight | 155104.49 |
| Authors | Mao, C.,Ealick, S.E. (deposition date: 1995-07-13, release date: 1996-06-20, Last modification date: 2024-02-07) |
| Primary citation | Mao, C.,Cook, W.J.,Zhou, M.,Koszalka, G.W.,Krenitsky, T.A.,Ealick, S.E. The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology. Structure, 5:1373-1383, 1997 Cited by PubMed Abstract: Purine nucleoside phosphorylase (PNP) from Escherichia coli is a hexameric enzyme that catalyzes the reversible phosphorolysis of 6-amino and 6-oxopurine (2'-deoxy)ribonucleosides to the free base and (2'-deoxy)ribose-1-phosphate. In contrast, human and bovine PNPs are trimeric and accept only 6-oxopurine nucleosides as substrates. The difference in the specificities of these two enzymes has been utilized in gene therapy treatments in which certain prodrugs are cleaved by E. coli PNP but not the human enzyme. The trimeric and hexameric PNPs show no similarity in amino acid sequence, even though they catalyze the same basic chemical reaction. Structural comparison of the active sites of mammalian and E. coli PNPs would provide an improved basis for the design of potential prodrugs that are specific for E. coli PNP. PubMed: 9351810DOI: 10.1016/S0969-2126(97)00287-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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