Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors
نویسندگان
چکیده
منابع مشابه
Metal stoichiometry and functional studies of the diphtheria toxin repressor.
Diphtheria toxin repressor (DtxR) is a transition metal ion-activated repressor in Corynebacterium diphtheriae. DtxR is an iron sensor; metal-bound DtxR represses transcription of genes downstream of the tox operator. Wild-type DtxR [DtxR(wt)] and several mutant forms were overexpressed and purified from Escherichia coli. DtxR was isolated without bound metal. Metal reconstitution gave a bindin...
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15 صفحه اولthe effects of changing roughness on the flow structure in the bends
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Short Communication: Diphtheria Toxin Repressor (dtxR) Gene-based Genetic Diversity of Corynebacterium diphtheriae isolated in Jakarta, Indonesia, 2018-2019
Background and Objective: In Indonesia, diphtheria cases caused by Corynebacterium diphtheriae are still occurring until today. One of the causes is probably the diphtheria toxin repressor (dtxR) gene which influences toxin expression. Therefore, in this study the characterization of the gene was performed to determine the mutations that affect the DtxR protein. Methods: The dtxR genes of ...
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The intact diphtheria toxin molecule, a single polypeptide chain of about 62,000 daltons, has no enzymic activity. However, the transfer in uifro of ADP-ribose from NAD to aminoacyltrensferase II can be catalyzed by any of several fragments of toxin. The smallest active fragment (A, 24,000 daltons) is normally connected to the remainder of the molecule (B, 38,000 daltons) by a peptide bond and ...
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ژورنال
عنوان ژورنال: Structure
سال: 1995
ISSN: 0969-2126
DOI: 10.1016/s0969-2126(01)00137-x