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PDBsum entry 3gfi

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Top Page protein dna_rna Protein-protein interface(s) links
Transcription/DNA PDB id
3gfi
Contents
Protein chains
143 a.a.
DNA/RNA
Waters ×154

References listed in PDB file
Key reference
Title St1710-Dna complex crystal structure reveals the DNA binding mechanism of the marr family of regulators.
Authors T.Kumarevel, T.Tanaka, T.Umehara, S.Yokoyama.
Ref. Nucleic Acids Res, 2009, 37, 4723-4735.
PubMed id 19509310
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.
Secondary reference #1
Title Crystal structure of the marr family regulatory protein, St1710, From sulfolobus tokodaii strain 7.
Authors T.Kumarevel, T.Tanaka, M.Nishio, S.C.Gopinath, K.Takio, A.Shinkai, P.K.Kumar, S.Yokoyama.
Ref. J Struct Biol, 2008, 161, 9.
PubMed id 17933554
Abstract
PROCHECK
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