1dup
From Proteopedia
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DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDO HYDROLASE (D-UTPASE)
Overview
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.
About this Structure
1DUP is a Single protein structure of sequence from Escherichia coli. Active as dUTP diphosphatase, with EC number 3.6.1.23 Full crystallographic information is available from OCA.
Reference
Crystal structure of a dUTPase., Cedergren-Zeppezauer ES, Larsson G, Nyman PO, Dauter Z, Wilson KS, Nature. 1992 Feb 20;355(6362):740-3. PMID:1311056
Page seeded by OCA on Tue Nov 20 13:36:01 2007
