The structure of PurR mutant L54M shows an alternative route to DNA kinking

The crystal structure of the purine repressor mutant L54M bound to hypoxanthine and to the purF operator provides a stereochemical understanding of the high DNA affinity of this hinge helix mutant. Comparison of the PurR L54M-DNA complex to that of the wild type PurR-DNA complex reveals that these p...

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Veröffentlicht in:Nature structural biology 1998-06, Vol.5 (6), p.436-441
Hauptverfasser: Arvidson, Dennis N, Lu, Fu, Faber, Catherine, Zalkin, Howard, Brennan, Richard G
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container_title Nature structural biology
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creator Arvidson, Dennis N
Lu, Fu
Faber, Catherine
Zalkin, Howard
Brennan, Richard G
description The crystal structure of the purine repressor mutant L54M bound to hypoxanthine and to the purF operator provides a stereochemical understanding of the high DNA affinity of this hinge helix mutant. Comparison of the PurR L54M-DNA complex to that of the wild type PurR-DNA complex reveals that these purine repressors bind and kink DNA similarly despite significant differences in their minor groove contacts and routes to interdigitation of the central C.G:G.C base pair step. Modeling studies, supported by genetic and biochemical data, show that the stereochemistry of the backbone atoms of the abutting hinge helices combined with the rigidity of the kinked base pair step constrain the interdigitating residue to leucine or methionine for the LacI/GalR family of transcription regulators.
doi_str_mv 10.1038/nsb0698-436
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subjects Amino Acid Substitution - genetics
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Crystallography, X-Ray
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - genetics
Leucine - genetics
Methionine - genetics
Models, Molecular
Mutagenesis, Site-Directed
Nucleic Acid Conformation
Protein Binding
Protein Folding
Protein Structure, Secondary
Repressor Proteins - chemistry
Repressor Proteins - genetics
title The structure of PurR mutant L54M shows an alternative route to DNA kinking
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