1DUP
DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDO HYDROLASE (D-UTPASE)
Summary for 1DUP
| Entry DOI | 10.2210/pdb1dup/pdb |
| Descriptor | DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE (2 entities in total) |
| Functional Keywords | hydrolase, nucleotide metabolism |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 16302.61 |
| Authors | Dauter, Z.,Wilson, K.S.,Larsson, G.,Nyman, P.O.,Cedergren, E. (deposition date: 1995-09-01, release date: 1995-11-14, Last modification date: 2024-02-07) |
| Primary citation | Cedergren-Zeppezauer, E.S.,Larsson, G.,Nyman, P.O.,Dauter, Z.,Wilson, K.S. Crystal structure of a dUTPase. Nature, 355:740-743, 1992 Cited by PubMed Abstract: The enzyme dUTPase catalyses the hydrolysis of dUTP and maintains a low intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. dUTPase from Escherichia coli is strictly specific for its dUTP substrate, the active site discriminating between nucleotides with respect to the sugar moiety as well as the pyrimidine base. Here we report the three-dimensional structure of E. coli dUTPase determined by X-ray crystallography at a resolution of 1.9 A. The enzyme is a symmetrical trimer, and of the 152 amino acid residues in the subunit, the first 136 are visible in the crystal structure. The tertiary structure resembles a jelly-roll fold and does not show the 'classical' nucleotide-binding domain. In the quaternary structure there is a complex interaction between the subunits that may be important in catalysis. This possibility is supported by the location of conserved elements in the sequence. PubMed: 1311056DOI: 10.1038/355740a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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