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PMID: 3903514 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

The three-dimensional structure of trp repressor.

Nature ·Vol. 317 ·No. 6040 ·1985-00-00 ·Pages 782-6

Schevitz RW, Otwinowski Z, Joachimiak A, Lawson CL, Sigler PB

Abstract

The crystal structure of the Escherichia coli trp repressor has been solved to atomic resolution. The dimeric protein has a remarkable subunit interface in which five of each subunit's six helices are interlinked. The binding of L-tryptophan activates the aporepressor indirectly by fixing the orientation of the second helix of the helix-turn-helix motif and by moulding the details of the repressor's structure near the DNA binding surface.

MeSH Terms

Bacterial Proteins Binding Sites Chemical Phenomena Chemistry Crystallization DNA, Bacterial/metabolism Escherichia coli Macromolecular Substances Models, Molecular Mutation Operator Regions, Genetic Protein Conformation Repressor Proteins/genetics,metabolism Transcription Factors/genetics,metabolism Tryptophan/metabolism

Chemicals

Bacterial Proteins DNA, Bacterial Macromolecular Substances Repressor Proteins TRPR protein, E coli Transcription Factors Tryptophan

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Schevitz R W

Otwinowski Z

Joachimiak A

Lawson C L

Sigler P B

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/317782a0

Published

1985-00-00

Pages

782-6

Language

English

Region

England

NLM ID

0410462

Subset

Grants

NIGMS NIH HHS · GM 07183 · United States

NIGMS NIH HHS · GM 15225 · United States

NCRR NIH HHS · S10 RRO1713 · United States

External Links

PubMed source DOI: 10.1038/317782a0 View journal details

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The three-dimensional structure of trp repressor.

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