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J Am Chem Soc. 2011 Dec 14;133(49):19614-7. doi: 10.1021/ja2080532. Epub 2011 Nov 21.

Crystal structure of the zinc-dependent MarR family transcriptional regulator AdcR in the Zn(II)-bound state.

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1
Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.

Abstract

Streptococcus pneumoniae adhesin competence regulator (AdcR), the first metal-dependent member of the multiple antibiotic resistance regulator (MarR) family of proteins, represses the transcription of a high-affinity zinc-specific uptake transporter, a group of surface antigen zinc-binding pneumococcal histidine triad proteins (PhtA, PhtB, PhtD, and PhtE), and an AdcA homologue (AdcAII). The 2.0 Å resolution structure of Zn(II)-bound AdcR reveals a highly helical two-fold-symmetric dimer with two distinct metal-binding sites per protomer. Zn(II) is tetrahedrally coordinated by E24, H42, H108, and H112 in what defines the primary sensing site in AdcR. Site 2 is a tetracoordinate site whose function is currently unknown. NMR methyl group perturbation experiments reveal that Zn(II) drives a global change in the structure of apo-AdcR that stabilizes a conformation that is compatible with DNA binding. This co-repression mechanism is unprecedented in MarR transcriptional regulators.

PMID:
22085181
PMCID:
PMC3246308
DOI:
10.1021/ja2080532
[Indexed for MEDLINE]
Free PMC Article

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