1BRW
THE CRYSTAL STRUCTURE OF PYRIMIDINE NUCLEOSIDE PHOSPHORYLASE IN A CLOSED CONFORMATION
Summary for 1BRW
| Entry DOI | 10.2210/pdb1brw/pdb |
| Descriptor | PROTEIN (PYRIMIDINE NUCLEOSIDE PHOSPHORYLASE), PHOSPHATE ION, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | nucleoside phosphorylase, domain movement, transferase |
| Biological source | Geobacillus stearothermophilus |
| Total number of polymer chains | 2 |
| Total formula weight | 92899.03 |
| Authors | Pugmire, M.J.,Ealick, S.E. (deposition date: 1998-08-25, release date: 1999-01-13, Last modification date: 2023-08-09) |
| Primary citation | Pugmire, M.J.,Ealick, S.E. The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation. Structure, 6:1467-1479, 1998 Cited by PubMed Abstract: Pyrimidine nucleoside phosphorylase (PYNP) catalyzes the reversible phosphorolysis of pyrimidines in the nucleotide synthesis salvage pathway. In lower organisms (e.g. Bacillus stearothermophilus) PYNP accepts both thymidine and uridine, whereas in mammalian and other higher organisms it is specific for thymidine (designated thymidine phosphorylase, TP). PYNP shares 40% sequence similarity (and presumably significant structural similarity) with human TP, which has been implicated as a growth factor in tumor angiogenesis. It is thought that TP undergoes a major conformational change upon substrate binding that consequently produces an active conformation. PubMed: 9817849DOI: 10.1016/S0969-2126(98)00145-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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