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Structure of IDP04634

Crystal Structure of Citrate Synthase from Francisella tularensis

Edit deposit information
CSGID target
IDP04634 
PDB Id
3MSU (NCBI MMDB
Authors
N.Maltseva,Y.Kim,J.Hasseman,W.F.Anderson,A.Joachimiak 
Responsible person
Natalia Maltseva 
Responsible lab
Argonne National Laboratory 
Deposition Date
Apr 29, 2010 
Release Date
May 26, 2010 

Annotation

Description
Citrate synthase is a member of a small family of enzymes that can directly form a carbon-carbon bond without the presence of metal ion cofactors. It catalyses the first reaction in the Krebs' cycle, namely the conversion of oxaloacetate and acetyl-coenzyme A into citrate and coenzyme A. This reaction is important for energy generation and for carbon assimilation. The reaction proceeds via a non-covalently bound citryl-coenzyme A intermediate in a 2-step process (aldol-Claisen condensation followed by the hydrolysis of citryl-CoA). The protein monomer is composed of two domains: a large alpha-helical domain consisting of two structural repeats, where the second repeat is interrupted by a small alpha-helical domain. The cleft between these domains forms the active site, where both citrate and acetyl-coenzyme A bind. The enzyme undergoes a conformational change upon binding of the oxaloacetate ligand, whereby the active site cleft closes over in order to form the acetyl-CoA binding site. Crystal Structure of Citrate Synthase from Francisella tularensis complexed with oxaloacetate ion was solved at 1.85A and represents dimer in the crystal. 
Functional assignment
 

Ligands

Ligand code Name Ligand type
TRS Tris(hydroxymethyl)aminomethane crystallization
OAA oxaloacetate ion biological
ZN
CL
SO4
ACY

Structure information

Unit cell parameters

Space Group
P 21 21 21  
Unit Cell

a=75.40Å, b=76.38Å, c=154.14Å
α=90.00, β=90.00, γ=90.00 
Solvent content
47.09  
Matthews coefficient
2.32  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
42.63-1.84Å (1.91-1.84Å)  
Rall(%)
16.2 
Rwork(%)
16.0 (19.8) 
Rfree(%)
20.0 (25.2) 
Num. observed reflections
80983 (7452) 
Num. Rfree reflections
4081 (378) 
Completeness(%)
99.4 (97.0) 

Model parameters

Num Atoms
7462  
Num Waters
580  
Num Hetatoms
66  
Model mean isotropic B factor
32.370Å2  
RMSD bond length
0.011Å  
RMSD bond angle
1.221°  
RMSD dihedral angle
17.54°
 
Filename uploaded
dep.pdb (uploaded on Apr 30, 2010 12:22 PM)  
Inserted
Apr 30, 2010