Structure of IDP91213

2.5 Angstrom Resolution Crystal Structure of Bifidobacterium longum Chorismate Synthase

Edit deposit information
CSGID target
IDP91213 
PDB Id
4ECD (NCBI MMDB
Authors
S.H.Light,G.Minasov,S.N.Krishna,L.Shuvalova,K.Kwon,A.Lavie,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Sam Light 
Responsible lab
Northwestern University 
Deposition Date
Mar 26, 2012 
Release Date
Apr 04, 2012 

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. Chorismate synthase is the final enzyme in the shikimate pathway and catalyzes the conversion of 5-enolpyruvyl-3-shikimate phosphate to chorismate. The enzyme forms a 4-layer sandwich. Nearly a quarter of the residues in the protein, many of which form a portion of the active site, are disordered.  
Functional assignment
 

Ligands

Ligand code Name Ligand type

Structure information

Unit cell parameters

Space Group
P 42 21 2  
Unit Cell

a=123.94Å, b=123.94Å, c=97.88Å
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
29.54-2.50Å (2.57-2.50Å)  
Rall(%)
20.0 
Rwork(%)
19.7 (27.8) 
Rfree(%)
25.3 (28.5) 
Num. observed reflections
26321 (1757) 
Num. Rfree reflections
1316 (87) 
Completeness(%)
97.6 (100.0) 

Model parameters

Num Atoms
4151  
Num Waters
133  
Num Hetatoms
0  
Model mean isotropic B factor
40.620Å2  
RMSD bond length
0.014Å  
RMSD bond angle
1.665°  
Filename uploaded
idp91213a_validate3.pdb (uploaded on Mar 26, 2012 3:31 PM)  
Inserted
Mar 26, 2012