PDBsum entry: 3gfi

Transcription/DNA

PDB id: 3gfi

Contents

Protein chains

143 a.a. *

DNA/RNA

Waters ×154

* Residue conservation analysis

PDB id:

3gfi

Name:

Transcription/DNA

Title:

Crystal structure of st1710 complexed with its promoter DNA

Structure:

146aa long hypothetical transcriptional regulator. Chain: a, c. Synonym: transcription regulator st1710. Engineered: yes. 5'-d( Tp Ap Ap Cp Ap Ap Tp Ap Gp Cp Ap Ap A)-3'. Chain: d. Engineered: yes. 5'-d( Tp Tp Gp Cp Tp Ap Tp Tp Gp T)-3'.

Source:

Sulfolobus tokodaii. Organism_taxid: 111955. Gene: st1710. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic: yes

Resolution:

2.10Å R-factor: 0.234 R-free: 0.280

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:

26-Feb-09 Release date: 25-Aug-09

Protein chains

Q96ZY1  (Q96ZY1_SULTO) -  Putative MarR family transcriptional regulator

Seq: 146 a.a.

Struc: 143 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: intracellular (1 term)
• Biological process: regulation of transcription (3 terms)
• Biochemical function: DNA binding (2 terms)

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.