1dup

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{{STRUCTURE_1dup| PDB=1dup | SCENE= }}
{{STRUCTURE_1dup| PDB=1dup | SCENE= }}
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'''DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDO HYDROLASE (D-UTPASE)'''
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===DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDO HYDROLASE (D-UTPASE)===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_1311056}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 1311056 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1311056}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Nucleotide metabolism]]
[[Category: Nucleotide metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:17:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:38:46 2008''

Revision as of 20:38, 30 June 2008

Template:STRUCTURE 1dup

DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDO HYDROLASE (D-UTPASE)

Template:ABSTRACT PUBMED 1311056

About this Structure

1DUP is a Single protein structure of sequence from Escherichia coli. 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

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