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Structure of IDP01842

2.20 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii

Edit deposit information
CSGID target
IDP01842 
PDB Id
3ROI (NCBI MMDB
Authors
S.H.Light,G.Minasov,S.N.Krishna,A.S.Halavaty,L.Shuvalova,L.Papazisi,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Sam Light 
Responsible lab
Northwestern University 
Deposition Date
Apr 25, 2011 
Release Date
May 18, 2011 

Annotation

Description
The shikimate pathway links metabolism of carbohydrates to biosynthesis of aromatic compounds. In a sequence of seven steps, phosphoenolpyruvate and erythrose 4-phosphate are converted to chorismate, a precursor of the aromatic amino acids and many secondary aromatic metabolites. The shikimate pathway is essential for most bacteria and plants but absent in humans, making it an attractive target for the development of novel antibiotics. 3-phosphoshikimate 1- carboxyvinyltransferase is the sixth enzyme in the shikimate pathway and catalyzes the conversion of shikimate-3-phosphate and phosphoenolpyruvate to 5-enolpyruvyl-3-shikimate phosphate. The enzyme consists of six βαβαββ motifs, three in both N- and C-terminal domains. In this unliganded structure the two domains are splayed outwards (more so than in reported homolog structures) and a unique domain-domain interface is observed. Additionally, there are significant structural differences in the position of two crucial negatively charged C-terminal active site residues, which are sequestered within secondary structure and removed from the active site.  
Functional assignment
 

Ligands

Ligand code Name Ligand type
CL crystallization
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
P 21 21 21  
Unit Cell

a=42.16Å, b=116.41Å, c=160.75Å
α=90.00, β=90.00, γ=90.00 
Solvent content
 
Matthews coefficient
 

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
29.10-2.20Å (2.26-2.20Å)  
Rall(%)
19.3 
Rwork(%)
19.1 (21.5) 
Rfree(%)
24.3 (28.8) 
Num. observed reflections
40903 (2786) 
Num. Rfree reflections
2045 (126) 
Completeness(%)
99.6 (94.6) 

Model parameters

Num Atoms
6471  
Num Waters
198  
Num Hetatoms
287  
Model mean isotropic B factor
48.290Å2  
RMSD bond length
0.011Å  
RMSD bond angle
1.372°  
Filename uploaded
3ROI.pdb (uploaded on May 18, 2011 1:05 PM)  
Inserted
May 18, 2011