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Structure of IDP00896

1.55 Angstrom Crystal Structure of an Acetyl Esterase from Salmonella typhimurium

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CSGID target
IDP00896 
PDB Id
3GA7 (NCBI MMDB) 
Authors
G.Minasov,Z.Wawrzak,J.Brunzelle,O.Onopriyenko,T.Skarina,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
Feb 16, 2009 
Release Date
Feb 24, 2009 

Annotation

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Description
Aes is the central regulator of the Escherichia coli maltose system. Aes catalyzes hydrolysis of p-nitrophenyl esters of fatty acids, preferring substrates with short (less than 8 in length) acyl chains. Aes binds to the maltose operon regulator, MalT, and inhibits MalT transcriptional activation activity in competition with its inducer, maltotriose. Aes also binds to alpha-galactosidase; this interaction stimulates Aes esterase activity and inhibits alpha-galactosidase, suggesting that Aes may have a physiological role in regulation of metabolism of carbohydrates. The enzyme is monomeric. The catalytic triad is predicted to comprise Ser165, Asp262, and His292. In the presented crystal structure of Acetyl Esterase from Salmonella typhimurium active site Ser-165 is phosphorylated.  
Functional assignment
Acetyl esterase 
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
    CL chloride ion crystallization
    SEP phosphoserine
    MSE selenomethionine modified residue

    Structure information

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    Unit cell parameters

    Space Group
    C 2 2 21  
    Unit Cell

    a=82.75Å, b=133.21Å, c=64.14Å
    α=90.00, β=90.00, γ=90.00  
    Solvent content
    47.52  
    Matthews coefficient
    2.34  

    Refinement

    Data for the highest resolution shell is in parentheses.
    Resolution range
    30.00-1.55Å (1.59-1.55Å)  
    Rall(%)
    14.0  
    Rwork(%)
    13.8 (16.2)  
    Rfree(%)
    17.7 (20.5)  
    Num. observed reflections
    51613 (3733)  
    Num. Rfree reflections
    2632 (201)  
    Completeness(%)
    99.6 (98.9)  

    Model parameters

    Num Atoms
    2755  
    Num Waters
    472  
    Num Hetatoms
    640  
    Model mean isotropic B factor (Å2)
    11.610  
    RMSD bond length (Å)
    0.010  
    RMSD bond angle
    1.320°  
    Filename uploaded
    rcsb051617.pdb (uploaded on Mar 18, 2009 5:40 PM)  
    Inserted
    Mar 18, 2009