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PDBsum entry 2zkz

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protein Protein-protein interface(s) links
Transcription PDB id
2zkz
Jmol
Contents
Protein chains
86 a.a. *
82 a.a. *
Waters ×79
* Residue conservation analysis
PDB id:
2zkz
Name: Transcription
Title: Crystal structure of the transcriptional repressor pagr of b anthracis
Structure: Transcriptional repressor pagr. Chain: a, b, c, d. Synonym: protective antigen repressor. Engineered: yes
Source: Bacillus anthracis. Organism_taxid: 1392. Gene: pagr, tcra. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.00Å     R-factor:   0.246     R-free:   0.266
Authors: H.Zhao,A.Volkov,V.H.Veldore,K.I.Varughese
Key ref: H.Zhao et al. (2010). Crystal structure of the transcriptional repressor PagR of Bacillus anthracis. Microbiology, 156, 385-391. PubMed id: 19926656
Date:
01-Apr-08     Release date:   07-Apr-09    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
O31178  (PAGR_BACAN) -  Transcriptional repressor PagR
Seq:
Struc:
99 a.a.
86 a.a.
Protein chain
Pfam   ArchSchema ?
O31178  (PAGR_BACAN) -  Transcriptional repressor PagR
Seq:
Struc:
99 a.a.
82 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     transcription, DNA-dependent   2 terms 
  Biochemical function     DNA binding     2 terms  

 

 
Microbiology 156:385-391 (2010)
PubMed id: 19926656  
 
 
Crystal structure of the transcriptional repressor PagR of Bacillus anthracis.
H.Zhao, A.Volkov, V.H.Veldore, J.A.Hoch, K.I.Varughese.
 
  ABSTRACT  
 
PagR is a transcriptional repressor in Bacillus anthracis that controls the chromosomal S-layer genes eag and sap, and downregulates the protective antigen pagA gene by direct binding to their promoter regions. The PagR protein sequence is similar to those of members of the ArsR repressor family involved in the repression of arsenate-resistance genes in numerous bacteria. The crystal structure of PagR was solved using multi-wavelength anomalous diffraction (MAD) techniques and was refined with 1.8 A resolution diffraction data. The PagR molecules form dimers, as observed in all SmtB/ArsR repressor family proteins. In the crystal lattice four PagR dimers pack together to form an inactive octamer. Model-building studies suggest that the dimer binds to a DNA duplex with a bend of around 4 degrees.