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Structure of IDP90922

1.85 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (aroD) from Salmonella typhimurium LT2.

Edit deposit information
CSGID target
IDP90922 
PDB Id
3L2I (NCBI MMDB
Authors
G.Minasov,S.H.Light,L.Shuvalova,L.Papazisi,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
George Minasov 
Responsible lab
Northwestern University 
Deposition Date
Dec 15, 2009 
Release Date
Dec 29, 2009 

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. The third step in the pathway consists of the dehydration of dehydroquinate to dehydroshikimate. This reaction can be achieved independently by two distinct enzyme families. The protein structure presented here is representative of the type I enzyme. The structure displays a typical TIM barrel fold with eight parallel beta strands and a C-terminal active site. In its unliganded form a three residues near the active site are disordered and have not been modeled. 
Functional assignment
 

Ligands

Ligand code Name Ligand type
MG magnesium ion crystallization

Structure information

Unit cell parameters

Space Group
P 21 21 21  
Unit Cell

a=36.92Å, b=76.91Å, c=171.85Å
α=90.00, β=90.00, γ=90.00 
Solvent content
39.3  
Matthews coefficient
2.03  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
28.64-1.85Å (1.90-1.85Å)  
Rall(%)
17.0 
Rwork(%)
16.8 (21.0) 
Rfree(%)
21.4 (29.1) 
Num. observed reflections
42787 (3010) 
Num. Rfree reflections
2139 (162) 
Completeness(%)
99.9 (98.6) 

Model parameters

Num Atoms
4119  
Num Waters
443  
Num Hetatoms
453  
Model mean isotropic B factor
17.920Å2  
RMSD bond length
0.016Å  
RMSD bond angle
1.526°  
Filename uploaded
rcsb056750.pdb (uploaded on Jan 06, 2010 12:53 PM)  
Inserted
Jan 06, 2010