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Diphtheria toxin repressor

Que, Q. and Helmann, J. D. (2000). Manganese homeostasis in Bacillus subtilis is regulated by MntR, a bifunctional regulator related to the diphtheria toxin repressor family of proteins, Mol. Microbiol., 35, 1454-1468. [Pg.334]

DtxR, C-terminal SH3-like domain from diphtheria toxin repressor, residues 144—226... [Pg.241]

Spiering MM, Ringe D, Murphy JR, Marietta MA. Metal stoichiometry and functional studies of the diphtheria toxin repressor. Proc. Natl. Acad. Sci. U.S.A. 2003 100 3808-3813. [Pg.1087]

Pohl E, Holmes RK, Hoi WGJ. 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. J. Biol. Chem. 1998 273 22420-22427. [Pg.1088]

White A, Ding X, vander Spek JC, Murphy JR, Ringe D. Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex. Nature 1998 394 502-506. [Pg.1088]

Page 1090 and page 1097 (Figure 27.25) is adapted from crystallographic coordinates deposited with the Protein Data Bank. PDB ID IDDN. White, A., Ding, X., Vanderspek, J. C., Murphy J. R., Ringe, D., Structure of the Metal-lon-Activated Diphtheria Toxin Repressor/Tox Operator Complex. Nature 394, pp. 502, (1998). [Pg.1188]

Figure 21-2 Three-dimensional structure of the inactive dimeric diphtheria toxin repressor, apo-DtxR [18]. The amino-terminus is labeled with NH2. The secondary structtire elements are represented by arrows for j -strands (numbers) and ribbons for a-helices (letters). Figure 21-2 Three-dimensional structure of the inactive dimeric diphtheria toxin repressor, apo-DtxR [18]. The amino-terminus is labeled with NH2. The secondary structtire elements are represented by arrows for j -strands (numbers) and ribbons for a-helices (letters).
White and Ringe (Chapter 21) describe a new, metal-dependent mode of protein-DNA interaction, which was revealed by X-ray crystallographic studies of the diphtheria toxin repressor (DtxR). This protein is activated in the presence of iron, an adaptative response of Corynebacterium diphtheriae to low iron concentrations. [Pg.389]

Ringe, D. White, A. Chen, S. Murphy, J. R. Diphtheria toxin repressor metal ion mediated control of transcription. In Handbook of Metalloproteins Messerschmidt, A., Ed. Wiley Chichester, UK, 2001, pp 929-938. [Pg.212]

Gonzalez de Peredo, A. Saint-Pierre, C. Latour, J. M. Michaud-Soret, 1. Forest, E. Conformational changes of the ferric uptake regulation protein upon metal activation and DNA binding First evidence of structural homologies with the diphtheria toxin repressor. J. Mol Biol 2001, 3/0(1), 83-91. [Pg.569]


See other pages where Diphtheria toxin repressor is mentioned: [Pg.2553]    [Pg.1087]    [Pg.2552]    [Pg.204]    [Pg.209]    [Pg.125]    [Pg.181]    [Pg.2553]    [Pg.1087]    [Pg.2552]    [Pg.204]    [Pg.209]    [Pg.125]    [Pg.181]    [Pg.114]    [Pg.132]    [Pg.2653]    [Pg.5124]    [Pg.359]    [Pg.365]    [Pg.2652]    [Pg.5123]   
See also in sourсe #XX -- [ Pg.180 ]




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