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Structure of IDP90293

2.75 Angstrom Crystal Structure of Enolase 1 from Toxoplasma gondii.

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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

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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  
Slides:
  • Asymmetric unit
  • Biological unit
  • B-factors distribution
  • B-factors distribution on the surface
  • Homolog superposition
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    secondary structure, N to C, molecule

    Ligands

    Ligand code Name Ligand type
    SO4 sulfate ion crystallization
    CL chloride ion crystallization

    Structure information

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    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 (Å2)
    37.590  
    RMSD bond length (Å)
    0.007  
    RMSD bond angle
    1.315°  
    Filename uploaded
    rcsb061562.pdb (uploaded on Sep 17, 2010 5:19 PM)  
    Inserted
    Sep 17, 2010