Motion of the DNA-binding Domain with Respect to the Core of the Diphtheria Toxin Repressor (DtxR) Revealed in the Crystal Structures of Apo- and Holo-DtxR
Open Access
- 1 August 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (35) , 22420-22427
- https://doi.org/10.1074/jbc.273.35.22420
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- The Role of Iron-Binding Proteins in the Survival of Pathogenic BacteriaAnnual Review of Nutrition, 1994
- Cloning, sequence, and footprint analysis of two promoter/operators from Corynebacterium diphtheriae that are regulated by the diphtheria toxin repressor (DtxR) and ironJournal of Bacteriology, 1994
- The Development of Awareness of Iron-Withholding DefensePerspectives in Biology and Medicine, 1993
- Cysteine-102 is positioned in the metal binding activation site of the Corynebacterium diphtheriae regulatory element DtxR.Proceedings of the National Academy of Sciences, 1993
- Analysis of diphtheria toxin repressor‐operator interactions and characterization of a mutant repressor with decreased binding activity for divalent metalsMolecular Microbiology, 1993
- Role of iron in regulation of virulence genesClinical Microbiology Reviews, 1993
- Purification and characterization of the diphtheria toxin repressor.Proceedings of the National Academy of Sciences, 1992
- Specific binding of the diphtheria tox regulatory element DtxR to the tox operator requires divalent heavy metal ions and a 9-base-pair interrupted palindromic sequence.Proceedings of the National Academy of Sciences, 1992
- Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae.Proceedings of the National Academy of Sciences, 1990
- Diphtheria ToxinAnnual Review of Biochemistry, 1977