Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDG

1 Nov 1998

Abstract excerpt

Uracil-DNA glycosylase (UDG), a key highly conserved DNA repair enzyme involved in uracil excision repair, was discovered in Escherichia coli . The Bacillus subtilis bacteriophage, PBS-1 and PBS-2, which contain dUMP residues in their DNA, express a UDG inhibitor protein, Ugi which binds to UDG very tightly to form a physiologically irreversible complex. The X-ray analysis of the E. coli UDG ( Ec UDG)-Ugi complex...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to DNA and Nucleic Acid Chemistry
Share to DNA Repair Mechanisms
Share to HIV/AIDS drug development and treatment

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 9776748
DOI: 10.1093/nar/26.21.4880

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDGPMID 9776748Read ↗

Mutational analysis of the uracil DNA glycosylase inhibitor protein and its interaction with Escherichia coli uracil DNA glycosylase.Semantic proximity Read ↗

Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase.Semantic proximity Read ↗

Crystal structure and functional insights into uracil-DNA glycosylase inhibition by phage Φ29 DNA mimic protein p56.Semantic proximity Read ↗

Contrasting effects of mutating active site residues, aspartic acid 64 and histidine 187 of Escherichia coli uracil-DNA glycosylase on uracil excision and interaction with an inhibitor protein.Semantic proximity Read ↗

Architecturally diverse proteins converge on an analogous mechanism to inactivate Uracil-DNA glycosylase.Semantic proximity Read ↗

A unique uracil-DNA binding protein of the uracil DNA glycosylase superfamily.Semantic proximity Read ↗

Mutational and structural analyses of UdgX: insights into the active site pocket architecture and its evolution.Semantic proximity Read ↗

Uracil DNA glycosylase (UDG) activities in Bradyrhizobium diazoefficiens: characterization of a new class of UDG with broad substrate specificity.Semantic proximity Read ↗

Novel dimeric structure of phage φ29-encoded protein p56: insights into uracil-DNA glycosylase inhibition.Semantic proximity Read ↗

Substitutions at tyrosine 66 of Escherichia coli uracil DNA glycosylase lead to characterization of an efficient enzyme that is recalcitrant to product inhibition.Semantic proximity Read ↗

A phage mechanism for selective nicking of dUMP-containing DNA.Semantic proximity Read ↗

The Escherichia coli protein YjjG is a house-cleaning nucleotidase in vivo.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.