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Structure of IDP01112

Crystal structure of chaperone CsaA form Bacillus anthracis str. Ames

Edit deposit information
CSGID target
IDP01112 
PDB Id
3G48 (NCBI MMDB
Authors
B.Nocek,M.Zhou,J.Stam,W.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Boguslaw Nocek 
Responsible lab
Argonne National Laboratory 
Deposition Date
Feb 03, 2009 
Release Date
Mar 03, 2009 

Annotation

Description
We have determined the 1.5 A crystal structure of the Bacillus Anthracis str. Ames 12 kDa CsaA protein. Asymmetric unit structure revealed two molecules forming tight dimmer, highly likely the functional unit. The structure of the monomer closely resembles fold of oligonucleotide-binding proteins (PF01588). The two identical cavities on the protein surface are likely to constitute the substrate binding sites. The CsaA protein from B. subtilis, close homolog of B. Anthracis, is characterized as a chaperone with export-related activities. 
Functional assignment
 

Ligands

Ligand code Name Ligand type
GOL
EDO
SO4

Structure information

Unit cell parameters

Space Group
P 21 21 21  
Unit Cell

a=39.36Å, b=67.56Å, c=74.64Å
α=90.00, β=90.00, γ=90.00 
Solvent content
39.27  
Matthews coefficient
2.03  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
40.00-1.50Å (1.54-1.50Å)  
Rall(%)
16.7 
Rwork(%)
16.6 (25.5) 
Rfree(%)
20.1 (27.7) 
Num. observed reflections
32171 (2000) 
Num. Rfree reflections
1640 (87) 
Completeness(%)
98.5 (84.8) 

Model parameters

Num Atoms
1964  
Num Waters
256  
Num Hetatoms
0  
Model mean isotropic B factor
8.350Å2  
RMSD bond length
0.020Å  
RMSD bond angle
1.745°  
Filename uploaded
IDP1112-fin-0203.pdb (uploaded on Feb 05, 2009 12:34 PM)  
Inserted
Feb 05, 2009