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Transcription PDB id
3gfm
Jmol
Contents
Protein chain
141 a.a. *
Metals
_CA
Waters ×127
* Residue conservation analysis
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.
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    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q96ZY1  (Q96ZY1_SULTO) -  Putative MarR family transcriptional regulator
Seq:
Struc: 		146 a.a.
141 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21432936 I.C.Perera, and A.Grove (2011).
MarR homologs with urate-binding signature.
  Protein Sci, 20, 621-629.  
20716550 I.C.Perera, and A.Grove (2010).
Molecular mechanisms of ligand-mediated attenuation of DNA binding by MarR family transcriptional regulators.
  J Mol Cell Biol, 2, 243-254.  
20421503 Y.M.Chang, W.Y.Jeng, T.P.Ko, Y.J.Yeh, C.K.Chen, and A.H.Wang (2010).
Structural study of TcaR and its complexes with multiple antibiotics from Staphylococcus epidermidis.
  Proc Natl Acad Sci U S A, 107, 8617-8622.
PDB codes: 3kp2 3kp3 3kp4 3kp5 3kp6 3kp7
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.