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1vko

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

    Title Crystal structure of inositol-3-phosphate synthase (ce21227) from Caenorhabditis elegans at 2.30 A resolution. To be published
    Site JCSG
    PDB Id 1vko Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1176,CE21227
    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 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.74 Rfactor 0.20035
    Waters
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    Solvent Content 55.04

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1vko
    1. Computational modeling of laminin N_terminal domains using sparse distance constraints from disulfide bonds and chemical cross_linking
    S Kalkhof, S Haehn, M Paulsson - Proteins: Structure, , 2010 - Wiley Online Library
     
    2. sll1981, an acetolactate synthase homologue of Synechocystis sp. PCC6803, functions as L-myo-inositol 1-phosphate synthase
    A Chatterjee, KG Dastidar, S Maitra, A Das-Chatterjee - Planta, 2006 - Springer
     

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    Protein Summary

    Inositol-3-phosphate synthase (ce21227) from Caenorhabditis elegans (PFAM:PF01658) catalyzes the conversion of D-glucose 6-phosphate to 1-L-myo-inositol-1-phosphate (MIP), the first and rate-limiting step in the biosynthesis of all inositol-containing compounds. Homologous sequences are distributed across all kingdoms of Life, but viruses. A two-reaction pathway is found for myo-inositol biosynthesis in all eukaryotic cells. First, glucose-6-phosphate is cyclized to form myo-inositol 1-phosphate, which is then dephosphorylated in the next step to produce free myo-inositol. These two steps are catalyzed by myo-inositol 1-phosphate synthase (EC:5.5.1.4) (IPS) and inositol monophosphatase (EC:3.1.3.25), respectively (PMID:12941308).

     

    Inositol-3-phosphate synthase (ce21227) from Caenorhabditis elegans has two structural domains: N-terminal domain with NAD(P)-binding Rossmann-fold (SCOP sunid:51734), and C-terminal domain with Glyceraldehyde-3-phosphate dehydrogenase-like fold (SCOP sunid:55346). The C-terminal domian belongs to dihydrodipicolinate reductase-like family (SCOP sunid:55368).

    Similar structures: PBD:1jkf, PDB:1u1i, PDB:1vjp, and PDB:1gr0.

    Ligand Summary

    References

    Reviews

    References

     

    No references found.

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