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Microbiology. 2010 Feb;156(Pt 2):385-91. doi: 10.1099/mic.0.033548-0. Epub 2009 Nov 19.

Crystal structure of the transcriptional repressor PagR of Bacillus anthracis.

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1
Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.

Abstract

PagR is a transcriptional repressor in Bacillus anthracis that controls the chromosomal S-layer genes eag and sap, and downregulates the protective antigen pagA gene by direct binding to their promoter regions. The PagR protein sequence is similar to those of members of the ArsR repressor family involved in the repression of arsenate-resistance genes in numerous bacteria. The crystal structure of PagR was solved using multi-wavelength anomalous diffraction (MAD) techniques and was refined with 1.8 A resolution diffraction data. The PagR molecules form dimers, as observed in all SmtB/ArsR repressor family proteins. In the crystal lattice four PagR dimers pack together to form an inactive octamer. Model-building studies suggest that the dimer binds to a DNA duplex with a bend of around 4 degrees.

PMID:
19926656
PMCID:
PMC2828352
DOI:
10.1099/mic.0.033548-0
[Indexed for MEDLINE]
Free PMC Article
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