1rn8: Difference between revisions

Revision as of 14:23, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1rn8.png

Template:STRUCTURE 1rn8

Crystal structure of dUTPase complexed with substrate analogue imido-dUTPCrystal structure of dUTPase complexed with substrate analogue imido-dUTP

Template:ABSTRACT PUBMED 15208312

About this StructureAbout this Structure

1RN8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase., Barabas O, Pongracz V, Kovari J, Wilmanns M, Vertessy BG, J Biol Chem. 2004 Oct 8;279(41):42907-15. Epub 2004 Jun 17. PMID:15208312

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of dUTPase complexed with substrate analogue imido-dUTP'''
+===Crystal structure of dUTPase complexed with substrate analogue imido-dUTP===
-==Overview==
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-dUTPase is essential to keep uracil out of DNA. Crystal structures of substrate (dUTP and alpha,beta-imino-dUTP) and product complexes of wild type and mutant dUTPases were determined to reveal how an enzyme responsible for DNA integrity functions. A kinetic analysis of wild type and mutant dUTPases was performed to obtain relevant mechanistic information in solution. Substrate hydrolysis is shown to be initiated via in-line nucleophile attack of a water molecule oriented by an activating conserved aspartate residue. Substrate binding in a catalytically competent conformation is achieved by (i) multiple interactions of the triphosphate moiety with catalysis-assisting Mg2+, (ii) a concerted motion of residues from three conserved enzyme motifs as compared with the apoenzyme, and (iii) an intricate hydrogen-bonding network that includes several water molecules in the active site. Results provide an understanding for the catalytic role of conserved residues in dUTPases.
+The line below this paragraph, {{ABSTRACT_PUBMED_15208312}}, adds the Publication Abstract to the page
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 [[Category: Enzyme-ligand complex]]
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