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Related Experiment Video

Updated: Jul 16, 2026

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes

Published on: November 1, 2012

Crystal structure of a dUTPase.

E S Cedergren-Zeppezauer¹, G Larsson, P O Nyman

¹Department of Zoological Cell Biology, Wenner-Gren Institute, University of Stockholm, Sweden.

|February 20, 1992

Summary

Escherichia coli dUTPase prevents uracil incorporation into DNA. X-ray crystallography reveals its 3D structure, showing a trimeric enzyme with a jelly-roll fold and complex subunit interactions potentially crucial for catalysis.

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Area of Science:

Biochemistry
Structural Biology
Enzymology

Background:

dUTPase enzymes prevent uracil incorporation into DNA by hydrolyzing dUTP.
Escherichia coli dUTPase exhibits strict substrate specificity, distinguishing nucleotides by sugar and base.
Maintaining low intracellular dUTP levels is critical for DNA integrity.

Purpose of the Study:

To determine the three-dimensional structure of Escherichia coli dUTPase.
To elucidate the structural basis for dUTPase's substrate specificity.
To investigate potential catalytic mechanisms based on structural features.

Main Methods:

X-ray crystallography was employed to determine the enzyme's structure.
High-resolution data collection at 1.9 Å.
Analysis of tertiary and quaternary structures.

Main Results:

The three-dimensional structure of E. coli dUTPase was resolved.
The enzyme forms a symmetrical trimer.
The tertiary structure features a jelly-roll fold, distinct from classical nucleotide-binding domains.
Complex subunit interactions within the quaternary structure were observed.
Conserved sequence elements are located in proximity to these interactions.

Conclusions:

The determined structure provides insights into the molecular architecture of E. coli dUTPase.
The unique structural features, including subunit interactions, may play a role in catalysis.
Further studies can explore the functional implications of these structural findings.