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2fp2

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary

    Title 1.6A Crystal Structure of the Secreted Chorismate Mutase from Mycobacterium tuberculosis: Novel Fold Topology Revealed. J.Mol.Biol. 357 1483-1499 2006
    Site TBSGC
    PDB Id 2fp2 Target Id
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    Related PDB Ids 2ao2 2f6l 2fp1 
    Molecular Characteristics
    Source
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    Alias Ids
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    TPS20726,15609022, O07746, 15609022, NP_216401.1
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.52 Rfactor 0.17016
    Waters
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    Solvent Content 51.14

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    Ligand Information
    Ligands TSA (8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-) x 1
    Metals

    Jmol

     
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    Google Scholar output for 2fp2

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    Protein Summary

     


    2FP2 is the crystal structure of Chorismate Mutase EC 5.4.99.5  in Mycobacterium Tuberculosis H37RV (Gene ID 885772). Chorismate Mutase catalyzes the interconversion of chorismate to perphenate through a claisen rearrangement.   The enzyme is negatively regulated by tyrosine, phenylalanine and tryptophan.

    The structure is a homodimer with each chain (see subunits) containing 162 amino acids.  Each subunit contains a Chorismate mutase type II fold that is entierly alpha helical with 6 alpha helices contained in the fold.  A strucutral alignment of the 2 subunits produced a RMSD value of 0.95 (see subunit overlap). Comparing the active subunit with the transition state analog shows alpha helice 2 and 4 moving towards one another (see subunit overlap).

    Subunits.GIFSubunit overlap.GIF

    The dimer interface consists of charged residues in one subunit forming salt bridges and hydrogen bonds to residues in the second subunit (see subunit interface 2) and large hydrophobic residues stacking (see subunit 1).   

     The active site contains four basic residues R49, K60, R72 and R134 ,two acidic residues E106 and E109, three polar residues Q76, T105, and S133, and three hydrophobic residues V56, L130, and I137 (see active site map). 

    Ligand Summary

    Reviews

    References

     

    No references found.

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