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Structure of IDP00456

2.05 Angstrom structure of a divalent-cation tolerance protein (CutA) from Yersinia pestis

Edit deposit information
CSGID target
IDP00456 
PDB Id
3GSD (NCBI MMDB
Authors
G.Minasov,Z.Wawrzak,T.Skarina,O.Onopriyenko,S.N.Peterson,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
George Minasov 
Responsible lab
Northwestern University 
Deposition Date
Mar 26, 2009 
Release Date
Apr 07, 2009 

Annotation

Description
CutA are a protein family present in bacteria, plants, and animals, including humans. Escherichia coli CutA is involved in copper tolerance, whereas mammalian proteins are implicated in the anchoring of acetylcholinesterase in neuronal cell membranes. Here we report crystal structure of the divalent-cation tolerance protein CutA from Yersinia pestis. Biological assembly is a homo trimer. Each subunit consists of a ferredoxin-like (beta1alpha1beta2beta3alpha2beta4) fold with an additional strand (beta5), a C-terminal helix (alpha3), and an unusual extended beta-hairpin involving strands beta2 and beta3. The evolutionarily conserved trimeric assembly of CutA is reminiscent of the architecture of PII signal transduction proteins. This similarity suggests an intriguing role of CutA proteins in signal transduction through allosteric communications between subunits. 
Functional assignment
Divalent-cation tolerance protein 

Ligands

Ligand code Name Ligand type
EPE crystallization
NA Sodium ion crystallization
PEG crystallization
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
C 2 2 21  
Unit Cell

a=140.78Å, b=157.91Å, c=157.13Å
α=90.00, β=90.00, γ=90.00 
Solvent content
54.21  
Matthews coefficient
2.69  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
29.59-2.05Å (2.10-2.05Å)  
Rall(%)
15.9 
Rwork(%)
15.6 (19.3) 
Rfree(%)
20.0 (25.7) 
Num. observed reflections
107278 (7579) 
Num. Rfree reflections
5363 (378) 
Completeness(%)
98.1 (95.0) 

Model parameters

Num Atoms
10549  
Num Waters
1187  
Num Hetatoms
1520  
Model mean isotropic B factor
26.160Å2  
RMSD bond length
0.011Å  
RMSD bond angle
1.209°  
Filename uploaded
rcsb052249.pdb (uploaded on Mar 27, 2009 7:04 PM)  
Inserted
Mar 27, 2009