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PMID: 1406951 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands.

Nature ·Vol. 359 ·No. 6394 ·1992-10-01 ·Pages 387-93

Somers WS, Phillips SE

Abstract

The crystal structure of the met repressor-operator complex shows two dimeric repressor molecules bound to adjacent sites 8 base pairs apart on an 18-base-pair DNA fragment. Sequence specificity is achieved by insertion of double-stranded antiparallel protein beta-ribbons into the major groove of B-form DNA, with direct hydrogen-bonding between amino-acid side chains and the base pairs. The repressor also recognizes sequence-dependent distortion or flexibility of the operator phosphate backbone, conferring specificity even for inaccessible base pairs.

MeSH Terms
Bacterial Proteins/chemistry,metabolism Base Sequence Crystallography DNA, Bacterial/chemistry Escherichia coli/genetics Escherichia coli Proteins Gene Expression Regulation, Bacterial/physiology Genes, Regulator Methionine/biosynthesis Molecular Conformation Molecular Sequence Data Operator Regions, Genetic/genetics Repressor Proteins/chemistry,metabolism
Chemicals
Bacterial Proteins DNA, Bacterial Escherichia coli Proteins Repressor Proteins methionine repressor protein, Bacteria methionine repressor protein, E coli Methionine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Somers W S
Department of Biochemistry and Molecular Biology, University of Leeds, UK.
Phillips S E
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1992-10-01
Pages
387-93
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
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