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Article

Flow linear dichroism and electron microscopic analysis of protein-DNA complexes of a mutant UvrB protein that binds to but cannot kink DNA.

Journal of molecular biology - 2 Sept 1994

Hsu D S, Takahashi M, Delagoutte E, Bertrand-Burggraf E, Wang Y H, Norden B, Fuchs R P, Griffith J, Sancar A

Abstract excerpt

(A)BC excinuclease of Escherichia coli is the enzymatic activity resulting from sequential and partially overlapping actions of UvrA, UvrB, and UvrC protein. UvrA is a molecular matchmaker which promotes the formation of a stable UvrB-damaged DNA complex in which the DNA is kinked by about 130 degrees. The UvrB-DNA complex is then recognized by UvrC and two incisions are made in the DNA by the joint actions of...

Topics

Adenosine Triphosphatases
Bacterial Proteins
DNA
DNA Helicases
DNA-Binding Proteins
Endodeoxyribonucleases
Escherichia coli Proteins
Microscopy, Electron
Mutation
Nucleic Acid Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Spectrophotometry, Ultraviolet

Ultraviolet Rays

Source

Identifiers

PMID: 8071991
DOI: 10.1006/jmbi.1994.1541

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8071991-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Flow linear dichroism and electron microscopic analysis of protein-DNA complexes of a mutant UvrB protein that binds to but cannot kink DNA.PMID 8071991Read ↗

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