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PMID: 8989318 Published · ppublish English Letter Research Support, Non-U.S. Gov't

Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site.

Nature structural biology ·Vol. 4 ·No. 1 ·1997-01-00 ·Pages 28-31

Kondo H, Nakagawa A, Nishihira J, Nishimura Y, Mizuno T, Tanaka I

Abstract

The C-terminal DNA-binding domain of OmpR, a positive regulator involved in osmoregulation expression of the ompF and ompC genes in Escherichia coli, has a helix-turn-helix variant motif. The 'turn' region, consisting of 11 residues, forms an RNA polymerase contact site.

MeSH Terms

Amino Acid Sequence Bacterial Outer Membrane Proteins/chemistry Binding Sites DNA-Binding Proteins/chemistry DNA-Directed RNA Polymerases/chemistry Escherichia coli/chemistry Helix-Turn-Helix Motifs Molecular Sequence Data Protein Structure, Secondary

Chemicals

Bacterial Outer Membrane Proteins DNA-Binding Proteins DNA-Directed RNA Polymerases

Authors & Affiliations

6 authors, click to expand affiliations / ORCID

Kondo H

Nakagawa A

Nishihira J

Nishimura Y

Mizuno T

Tanaka I

Article Info

Journal

Nature structural biology

Abbr.

Nat Struct Biol

ISSN

1072-8368

DOI

10.1038/nsb0197-28

Published

1997-01-00

Pages

28-31

Language

English

Region

United States

NLM ID

9421566

Subset

External Links

PubMed source DOI: 10.1038/nsb0197-28

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Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site.

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