1887

Abstract

PagR is a transcriptional repressor in that controls the chromosomal S-layer genes and , and downregulates the protective antigen 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 Å 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 °.

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2010-02-01
2019-10-20
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vol. , part 2, pp. 385 - 391

Sequence alignment (CLUSTALW) of PagR with other members of SmtB/ArsR family of proteins. Conserved residues R29, S59, L62 and Y81 are shown in bold. The helices and β-strands are highlighted. [ PDF] (49 kb)



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