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Structure of IDP02616

DNA-binding transcriptional repressor AcrR from Salmonella typhimurium.

Edit deposit information
CSGID target
IDP02616 
PDB Id
3LHQ (NCBI MMDB
Authors
J.Osipiuk,R.Mulligan,L.Papazisi,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Jerzy Osipiuk 
Responsible lab
Argonne National Laboratory 
Deposition Date
Jan 22, 2010 
Release Date
Feb 02, 2010 

Annotation

Description
The AcrR protein represses transcription of the acrAB operon which encodes the periplasmic membrane fusion protein AcrA and the multidrug efflux pump AcrB. AcrB is a multidrug transporter that belongs to the resistance-nodulation-division (RND) superfamily of MDR pumps. AcrB possesses a wide range of ligand recognition, including most of the currently administered antibiotics, chemotherapeutic agents, bile salts, dyes, and detergents. AcrB functions in conjunction with AcrA and TolC, the outer membrane channel protein. The AcrR N-terminal sequence shares similarity to the TetR family of transcriptional repressors. Like other members in this family, the N-terminal domain of AcrR contains a predicted DNA-binding helix-turn-helix (HTH) motif. The C-terminal domain has unique sequences and is expected to form a multi-drug binding site for its inducing drugs. Recent studies indicate that AcrR interacts with the same set of antimicrobial agents as AcrB with similar affinities. Binding a drug to the C-terminal ligand-binding domain of AcrR presumably triggers conformational change in its N-terminal DNA-binding region. This change results in the release of AcrR from its operator DNA, and thus allows transcription from its cognate promoter.  
Functional assignment
 

Ligands

Ligand code Name Ligand type
PEG
EDO

Structure information

Unit cell parameters

Space Group
P 1 21 1  
Unit Cell

a=47.18Å, b=75.82Å, c=55.18Å
α=90.00, β=108.67, γ=90.00 
Solvent content
33.68  
Matthews coefficient
1.85  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
38.00-1.56Å (1.60-1.56Å)  
Rall(%)
15.3 
Rwork(%)
15.0 (26.4) 
Rfree(%)
19.9 (35.2) 
Num. observed reflections
50990 (3372) 
Num. Rfree reflections
2600 (165) 
Completeness(%)
97.5 (88.0) 

Model parameters

Num Atoms
3951  
Num Waters
280  
Num Hetatoms
0  
Model mean isotropic B factor
15.400Å2  
RMSD bond length
0.020Å  
RMSD bond angle
1.643°  
Filename uploaded
idp02616.pdb (uploaded on Jan 22, 2010 8:14 PM)  
Inserted
Jan 22, 2010