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PMID: 9406544 Published · ppublish English Letter Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Dimerization of the UmuD' protein in solution and its implications for regulation of SOS mutagenesis.

Nature structural biology ·Vol. 4 ·No. 12 ·1997-12-00 ·Pages 979-83

Ferentz AE, Opperman T, Walker GC, Wagner G

Abstract

NMR spectroscopy has been used to determine that the dimerization interface of UmuD' in solution is not the homodimer interface originally inferred from crystallographic data. Instead, it resembles an interface that had been hypothesized to be involved in filamentation.

MeSH Terms

Bacterial Proteins/chemistry,genetics DNA-Directed DNA Polymerase Dimerization Escherichia coli/genetics,metabolism Escherichia coli Proteins Magnetic Resonance Spectroscopy Models, Molecular Mutagenesis Protein Conformation SOS Response, Genetics/genetics Solutions

Chemicals

Bacterial Proteins Escherichia coli Proteins Solutions DNA-Directed DNA Polymerase UmuD protein, E coli

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Ferentz A E

Opperman T

Walker G C

Wagner G

Article Info

Journal

Nature structural biology

Abbr.

Nat Struct Biol

ISSN

1072-8368

DOI

10.1038/nsb1297-979

Published

1997-12-00

Pages

979-83

Language

English

Region

United States

NLM ID

9421566

Subset

External Links

PubMed source DOI: 10.1038/nsb1297-979

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Dimerization of the UmuD' protein in solution and its implications for regulation of SOS mutagenesis.

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