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Publication Abstract from PubMed

ST1710, a member of the multiple antibiotic resistance regulator (MarR) family of regulatory proteins in bacteria and archaea, plays important roles in development of antibiotic resistance, a global health problem. Here, we present the crystal structure of ST1710 from Sulfolobus tokodaii strain 7 complexed with salicylate, a well-known inhibitor of MarR proteins and the ST1710 complex with its promoter DNA, refined to 1.8 and 2.10 A resolutions, respectively. The ST1710-DNA complex shares the topology of apo-ST1710 and MarR proteins, with each subunit containing a winged helix-turn-helix (wHtH) DNA binding motif. Significantly large conformational changes occurred upon DNA binding and in each of the dimeric monomers in the asymmetric unit of the ST1710-DNA complex. Conserved wHtH loop residues interacting with the bound DNA and mutagenic analysis indicated that R89, R90 and K91 were important for DNA recognition. Significantly, the bound DNA exhibited a new binding mechanism.

ST1710-DNA complex crystal structure reveals the DNA binding mechanism of the MarR family of regulators.,Kumarevel T, Tanaka T, Umehara T, Yokoyama S Nucleic Acids Res. 2009 Aug;37(14):4723-35. Epub 2009 Jun 9. PMID:19509310^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.