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.
journal_name
Proc Natl Acad Sci U S Aauthors
Schiering N,Tao X,Zeng H,Murphy JR,Petsko GA,Ringe Ddoi
10.1073/pnas.92.21.9843subject
Has Abstractpub_date
1995-10-10 00:00:00pages
9843-50issue
21eissn
0027-8424issn
1091-6490journal_volume
92pub_type
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