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PDBsum entry 2d6y

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protein ligands Protein-protein interface(s) links
Gene regulation PDB id
2d6y

 

 

 

 

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Contents
Protein chains
186 a.a. *
Ligands
TLA ×2
Waters ×154
* Residue conservation analysis
PDB id:
2d6y
Name: Gene regulation
Title: Crystal structure of transcriptional factor sco4008 from streptomyces coelicolor a3(2)
Structure: Putative tetr family regulatory protein. Chain: a, b. Synonym: putative transcriptional regulator. Engineered: yes
Source: Streptomyces coelicolor. Organism_taxid: 100226. Strain: a3(2). Gene: sco4008. Expressed in: rhodococcus erythropolis. Expression_system_taxid: 1833.
Biol. unit: Dimer (from PQS)
Resolution:
2.30Å     R-factor:   0.207     R-free:   0.259
Authors: T.Hayashi,Y.Tanaka,N.Sakai,M.Yao,T.Tamura,I.Tanaka
Key ref: T.Hayashi et al. (2013). SCO4008, a putative TetR transcriptional repressor from Streptomyces coelicolor A3(2), regulates transcription of sco4007 by multidrug recognition. J Mol Biol, 425, 3289-3300. PubMed id: 23831227 DOI: 10.1016/j.jmb.2013.06.013
Date:
15-Nov-05     Release date:   31-Oct-06    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9ADP7  (HTHR_STRCO) -  HTH-type transcriptional repressor SCO4008 from Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Seq:
Struc:
192 a.a.
186 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.jmb.2013.06.013 J Mol Biol 425:3289-3300 (2013)
PubMed id: 23831227  
 
 
SCO4008, a putative TetR transcriptional repressor from Streptomyces coelicolor A3(2), regulates transcription of sco4007 by multidrug recognition.
T.Hayashi, Y.Tanaka, N.Sakai, U.Okada, M.Yao, N.Watanabe, T.Tamura, I.Tanaka.
 
  ABSTRACT  
 
SCO4008 from Streptomyces coelicolor A3(2) is a member of the TetR family. However, its precise function is not yet clear. In this study, the crystal structure of SCO4008 was determined at a resolution of 2.3Å, and its DNA-binding properties were analyzed. Crystal structure analysis showed that SCO4008 forms an Ω-shaped homodimer in which the monomer is composed of an N-terminal DNA-binding domain containing a helix-turn-helix and a C-terminal dimerization and regulatory domain possessing a ligand-binding cavity. The genomic systematic evolution of ligands by exponential enrichment and electrophoretic mobility shift assay revealed that four SCO4008 dimers bind to the two operator regions located between sco4008 and sco4007, a secondary transporter belonging to the major facilitator superfamily. Ligand screening analysis showed that SCO4008 recognizes a wide range of structurally dissimilar cationic and hydrophobic compounds. These results suggested that SCO4008 is a transcriptional repressor of sco4007 responsible for the multidrug resistance system in S. coelicolor A3(2).
 

 

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