Crystal Structure of a σ 70 Subunit Fragment from E. coli RNA Polymerase

The 2.6 Å crystal structure of a fragment of the σ 70 promoter specificity subunit of E. coli RNA polymerase is described. Residues involved in core RNA polymerase binding lie on one face of the structure. On the opposite face, aligned along one helix, are exposed residues that interact with the −10...

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Bibliographic Details
Published in:Cell 1996-10, Vol.87 (1), p.127-136
Main Authors: Malhotra, Arun, Severinova, Elena, Darst, Seth A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Conserved Sequence
Crystallography, X-Ray
DNA, Bacterial - chemistry
DNA, Bacterial - genetics
DNA, Bacterial - metabolism
DNA-Directed RNA Polymerases - chemistry
DNA-Directed RNA Polymerases - genetics
DNA-Directed RNA Polymerases - metabolism
Escherichia coli - enzymology
Models, Molecular
Molecular Sequence Data
Mutation
Nucleic Acid Denaturation
Promoter Regions, Genetic - genetics
Protein Binding
Protein Conformation
Sigma Factor - chemistry
Sigma Factor - genetics
Sigma Factor - metabolism
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Description
Summary:The 2.6 Å crystal structure of a fragment of the σ 70 promoter specificity subunit of E. coli RNA polymerase is described. Residues involved in core RNA polymerase binding lie on one face of the structure. On the opposite face, aligned along one helix, are exposed residues that interact with the −10 consensus promoter element (the Pribnow box), including four aromatic residues involved in promoter melting. The structure suggests one way in which DNA interactions may be inhibited in the absence of RNA polymerase and provides a framework for the interpretation of a large number of genetic and biochemical analyses.
ISSN:0092-8674
1097-4172
DOI:10.1016/S0092-8674(00)81329-X