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Structure of IDP00956

2.0 Angstrom Crystal Structure of an Acyl Carrier Protein S-malonyltransferase from Salmonella typhimurium.

Edit deposit information
CSGID target
IDP00956 
PDB Id
3H0P (NCBI MMDB
Authors
G.Minasov,Z.Wawrzak,T.Skarina,O.Onopriyenko,S.N.Peterson,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
George Minasov 
Responsible lab
Northwestern University 
Deposition Date
Apr 10, 2009 
Release Date
Apr 21, 2009 

Annotation

Description
Malonyl-CoA-acyl carrier protein transacylase is a key enzyme in the fatty-acid biosynthesis pathway of bacteria. Endogenous fatty acids are synthesized in all organisms in a pathway catalyzed by the fatty acid synthase complex. In bacteria, where the fatty acids are used primarily for incorporation into components of cell membranes, fatty acid synthase is made up of several independent cytoplasmic enzymes, each catalyzing one specific reaction. The initiation of the elongation step, which extends the length of the growing acyl chain by two carbons, requires the transfer of the malonyl moiety from malonyl-CoA onto the acyl carrier protein. The acyl carrier protein from Salmonella Typhimurium is similar to one from Escherichia coli. The protein has an alpha/beta type architecture, but its fold is unique. The active site inferred from the location of the catalytic Ser-92 contains a typical nucleophilic elbow as observed in alpha/beta hydrolases. Various binary complex structures of the Escherichia coli enzyme are reported. The obtained data from structural studies could be used in aiding the process of rational inhibitor design. 
Functional assignment
Acyl carrier protein S-malonyltransferase  

Ligands

Ligand code Name Ligand type
MSE modified residue
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
P 1 21 1  
Unit Cell

a=46.59Å, b=92.17Å, c=77.08Å
α=90.00, β=92.84, γ=90.00 
Solvent content
50.7  
Matthews coefficient
2.49  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
29.54-2.00Å (2.05-2.00Å)  
Rall(%)
19.2 
Rwork(%)
19.0 (21.2) 
Rfree(%)
24.3 (27.6) 
Num. observed reflections
41793 (2916) 
Num. Rfree reflections
2089 (144) 
Completeness(%)
95.1 (91.3) 

Model parameters

Num Atoms
4927  
Num Waters
443  
Num Hetatoms
144  
Model mean isotropic B factor
12.370Å2  
RMSD bond length
0.012Å  
RMSD bond angle
1.260°  
Filename uploaded
idp00956.pdb (uploaded on Apr 10, 2009 1:06 AM)  
Inserted
Apr 10, 2009