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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacterial Proteins*
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Binding Sites
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Chemical Phenomena
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Chemistry
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Crystallization
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DNA, Bacterial / metabolism
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Escherichia coli
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Macromolecular Substances
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Models, Molecular
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Mutation
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Operator Regions, Genetic
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Protein Conformation
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Repressor Proteins* / genetics
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Repressor Proteins* / metabolism
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Transcription Factors* / genetics
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Transcription Factors* / metabolism
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Tryptophan / metabolism
Substances
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Bacterial Proteins
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DNA, Bacterial
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Macromolecular Substances
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Repressor Proteins
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TRPR protein, E coli
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Transcription Factors
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Tryptophan