Protein Science · 2000 · 15 citations · 13 references
Life SciencesGeneticsMolecular GeneticsGenetic EngineeringMicrobial GeneticsStructural BiologyBacterial Gene RegulationThermostable EnzymesBacterial MutationGlycine ReplacementResistance-suppressing MutationsTemperature SensitivityTemperature-sensitive MutantsThermostability Mechanisms
Escherichia coli strain LE316 contains a mutation in gyrB that results in the substitution of Val164 to Gly and confers both chlorobiocin resistance and temperature sensitivity. Selection for suppressors of the ts phenotype yielded second-site mutations in GyrB at His38 and Thr157. The properties of proteins bearing these mutations have been characterized, and a mechanism of suppression is proposed based upon structural considerations.
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Crystal structure of an N-terminal fragment of the DNA gyrase B protein
Dale B. Wigley, G.J. Davies, E.J. Dodson et al. · Nature · 1991 · 524 citations