ST1710-DNA complex crystal structure reveals the DNA binding mechanism of the MarR family of regulators.

Abstract:

: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.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Kumarevel T,Tanaka T,Umehara T,Yokoyama S

doi

10.1093/nar/gkp496

subject

Has Abstract

pub_date

2009-08-01 00:00:00

pages

4723-35

issue

14

eissn

0305-1048

issn

1362-4962

pii

gkp496

journal_volume

37

pub_type

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