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Anion-Coordinating Residues at Binding Site 1 Are Essential for the Biological Activity of the Diphtheria Toxin Repressor

The homodimeric diphtheria toxin repressor (DtxR) uses Fe(2+) as a corepressor, binds to iron-regulated promoters, and negatively regulates the syntheses of diphtheria toxin, corynebacterial siderophore, and several other Corynebacterium diphtheriae products. The crystal structure of DtxR shows that...

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Detalhes bibliográficos
Main Authors: Goranson-Siekierke, Joanne, Pohl, Ehmke, Hol, Wim G. J., Holmes, Randall K.
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Microbiology 1999
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC96531/
https://ncbi.nlm.nih.gov/pubmed/10085021
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