Structure of IDP90922

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

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

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

 

Matthews coefficient

 

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

28.64-1.85Å (1.90-1.85Å)  

R_all(%)

17.0  

R_work(%)

16.8 (21.0)  

R_free(%)

21.4 (29.1)  

Num. observed reflections

42787 (3010)  

Num. R_free reflections

2139 (162)  

Completeness(%)

99.9 (98.6)  

Model parameters

Num Atoms

4572  

Num Waters

443  

Num Hetatoms

1  

Model mean isotropic B factor

17.920Ų  

RMSD bond length

0.016Å  

RMSD bond angle

1.526°  

Filename uploaded

rcsb056750.pdb (uploaded on 2010-01-06 12:53:16-05)