PDBsum entry: 3gfm

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PDB-id: 3gfm

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Protein chain

141 a.a. *

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_CA

Waters ×127

* Residue conservation analysis

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• PDB id: 3gfm
• Name: Transcription
• Title: Crystal structure of the st1710 mutant (k91a) protein
• Structure: 146aa long hypothetical transcriptional regulator. Chain: a. Synonym: transcription regulator st1710. Engineered: yes. Mutation: yes
• Source: Sulfolobus tokodaii. Organism_taxid: 111955. Gene: st1710. Expressed in: escherichia coli. Expression_system_taxid: 562.

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()

• Resolution: 2.10Å
• R-factor: 0.218
• R-free: 0.270
• Authors: T.Kumarevel,T.Tanaka,S.Yokoyama
• Key ref: T.Kumarevel et al. (2009). ST1710-DNA complex crystal structure reveals the DNA binding mechanism of the MarR family of regulators.. Nucleic Acids Res, 37, 4723-4735. [PubMed id: 19509310] [DOI: 10.1093/nar/gkp496]
• Date: 27-Feb-09
• Release date: 25-Aug-09
• Related entries: 2eb7 ; native form ; 2yr2 ; crystal belong to different space group ; 3gez ; native form ; 3gf2 ; st1710-salicylate complex ; 3gfi ; st1710-DNA complex ; ... plus others (see Header records)

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Key reference

DOI no: 10.1093/nar/gkp496

Nucleic Acids Res 37:4723-4735 (2009)

PubMed id: 19509310

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

T.Kumarevel, T.Tanaka, T.Umehara, S.Yokoyama.

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.