1DPR

STRUCTURES OF THE APO-AND METAL ION ACTIVATED FORMS OF THE DIPHTHERIA TOX REPRESSOR FROM CORYNEBACTERIUM DIPHTHERIAE

Summary for 1DPR

• Entry DOI: 10.2210/pdb1dpr/pdb
• Descriptor: DIPHTHERIA TOX REPRESSOR (1 entity in total)
• Functional Keywords: diphtheria, virulence, dna-binding, iron-regulation repressor, transcription regulation
• Biological source: Corynebacterium diphtheriae
• Total number of polymer chains: 2
• Total formula weight: 50699.59

Authors

Schiering, N.,Tao, X.,Murphy, J.,Petsko, G.A.,Ringe, D. (deposition date: 1995-02-06, release date: 1995-09-15, Last modification date: 2024-02-07)

Primary citation

Schiering, N.,Tao, X.,Zeng, H.,Murphy, J.R.,Petsko, G.A.,Ringe, D.
Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae.
Proc.Natl.Acad.Sci.USA, 92:9843-9850, 1995

PubMed Abstract: The diphtheria tox repressor (DtxR) of Corynebacterium diphtheriae plays a critical role in the regulation of diphtheria toxin expression and the control of other iron-sensitive genes. The crystal structures of apo-DtxR and of the metal ion-activated form of the repressor have been solved and used to identify motifs involved in DNA and metal ion binding. Residues involved in binding of the activated repressor to the diphtheria tox operator, glutamine 43, arginine 47, and arginine 50, were located and confirmed by site-directed mutagenesis. Previous biochemical and genetic data can be explained in terms of these structures. Conformational differences between apo- and Ni-DtxR are discussed with regard to the mechanism of action of this repressor.

PubMed: 7568230
DOI: 10.1073/pnas.92.21.9843

Experimental method

X-RAY DIFFRACTION (3 Å)