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Structure of IDP90293

2.75 Angstrom Crystal Structure of Enolase 1 from Toxoplasma gondii.

Edit deposit information
CSGID target
IDP90293 
PDB Id
3OTR (NCBI MMDB
Authors
G.Minasov,J.Ruan,L.Shuvalova,A.Halavaty,H.Ngo,S.Tomavo,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
George Minasov 
Responsible lab
Northwestern University 
Deposition Date
Sep 13, 2010 
Release Date
Sep 22, 2010 

Annotation

Description
Enolase (EC 4.2.1.11, 2-phosphoglycerate dehydratase) catalysis the ninth and penultimate step of glycolysis which is the conversion of 2-phosphoglycerate to phosphoenolpyruvate. Toxoplasma gondii encodes two isoforms of such glycolytic enzymes, enolase 1 and enolase 2 that are expressed exclusively in bradyzoites and tachyzoites, respectively. The brain cysts specific TgEnolase 1 of the slow growing bradyzoites has been implicated as an attributed target in drug development for Toxoplasmosis. Despite its sequence similarity to other enolases, the TgEnolase 1 dimmer structure exhibits distinct surface properties. The EWGWS pentapeptide insertion and insertions in catalytic loops (loop 3) separate TgEnolase from the host human neuron specific enolase (hENO2, PDB code 1TE6). The C’-terminal KSGSPCRSERLCKYNQLMR sequences of each TgEnolase 1 monomers create a positively charged area that may correspond to the unique DNA binding function of TgEnolase1. These features indicate the role of TgEnolase 1 in the important pathogen T. gondii. 
Functional assignment
Enolase  

Ligands

Ligand code Name Ligand type
CL CHLORIDE ION crystallization
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
I 4  
Unit Cell

a=323.63Å, b=323.63Å, c=66.77Å
α=90.00, β=90.00, γ=90.00 
Solvent content
58.23  
Matthews coefficient
2.94  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
29.55-2.75Å (2.82-2.75Å)  
Rall(%)
17.3 
Rwork(%)
17.1 (25.7) 
Rfree(%)
21.9 (32.7) 
Num. observed reflections
90657 (6624) 
Num. Rfree reflections
4532 (344) 
Completeness(%)
100.0 (100.0) 

Model parameters

Num Atoms
20363  
Num Waters
578  
Num Hetatoms
584  
Model mean isotropic B factor
37.590Å2  
RMSD bond length
0.007Å  
RMSD bond angle
1.315°  
Filename uploaded
rcsb061562.pdb (uploaded on Sep 17, 2010 5:19 PM)  
Inserted
Sep 17, 2010