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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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| Auteurs principaux: | , , , |
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| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
American Society for Microbiology
1999
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC96531/ https://ncbi.nlm.nih.gov/pubmed/10085021 |
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