1dpr
From Proteopedia
STRUCTURES OF THE APO-AND METAL ION ACTIVATED FORMS OF THE DIPHTHERIA TOX REPRESSOR FROM CORYNEBACTERIUM DIPHTHERIAE
Overview
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.
About this Structure
1DPR is a Single protein structure of sequence from Corynebacterium diphtheriae. Full crystallographic information is available from OCA.
Reference
Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae., Schiering N, Tao X, Zeng H, Murphy JR, Petsko GA, Ringe D, Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9843-50. PMID:7568230 Page seeded by OCA on Fri May 2 14:07:40 2008
