Annotation

Description

The 1.6 Å resolution structure of the Vibrio vulnificus arginine repressor was determined by molecular replacement using two models: (i) C-terminal domain of Escherichia coli arginine repressor/L-arginine complex (PDB code 1XXB); and (ii) the Reovirus outer capsid protein Sigma (3PDB code 1FN9). The first model was successful in finding a structure solution for a C-terminal domain of the protein, whereas the second structure was useful in finding solution for a N-terminal domain of the arginine repressor. The asymmetric unit is comprised of a single polypeptide chain with an alpha/beta fold. The N-terminal domain has three antiparallel helices and a two-stranded antiparallel β-sheet. The C-terminal domain contains a four-stranded antiparallel β-sheet and three antiparallel helices. Residues 71-76 that link the two domains are disordered in the structure. The C-terminal domain sits on a 3-fold crystallographic axis creating a trimer (buried surface area is 4380 Å2) with another two symmetry-related molecules. Another possible oligomer in the crystal is a hexamer (buried surface area is 14430 Å2) that is formed from two trimers positioned back-to-back along the aforementioned axis. 

Functional assignment

DNA BINDING PROTEIN 

Structure information

Unit cell parameters

Space Group

P 63 2 2  

Unit Cell

a=73.31Å, b=73.31Å, c=118.60Å
α=90.00, β=90.00, γ=120.00 

Solvent content

 

Matthews coefficient

 

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

29.65-1.60Å (1.64-1.60Å)  

R_all(%)

18.2 

R_work(%)

18.2 (21.8) 

R_free(%)

19.8 (27.0) 

Num. observed reflections

25557 (1828) 

Num. R_free reflections

1303 (87) 

Completeness(%)

100.0 (100.0) 

Model parameters

Num Atoms

1257  

Num Waters

176  

Num Hetatoms

184  

Model mean isotropic B factor

23.940Ų  

RMSD bond length

0.008Å  

RMSD bond angle

1.602°  

Filename uploaded

3V4G.pdb (uploaded on Jan 10, 2012 12:27 PM)  

Inserted

Dec 26, 2011