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1vlr

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

    Title Crystal structure of an Apo mRNA decapping enzyme (DcpS) from Mouse at 1.83 A resolution. Proteins 60 797-802 2005
    Site JCSG
    PDB Id 1vlr Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1341,16740816, 89679, 89708, 282285, 282426, 289400, 289403, 289431
    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 2.35 Rfactor 0.15838
    Waters
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    Solvent Content 47.29

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1vlr
    1. Processing the message: structural insights into capping and decapping mRNA
    M Gu, CD Lima - Current opinion in structural biology, 2005 - Elsevier
     
    2. Crystal structure of an Apo mRNA decapping enzyme (DcpS) from Mouse at 1.83 resolution
    GW Han, R Schwarzenbacher - Proteins: Structure, , 2005 - Wiley Online Library
     
    3. Applications of Bioinformatics to Protein Structures: How Protein Structure and Bioinformatics Overlap
    GW Han, C Rife, MR Sawaya - Methods in Molecular Biology, 2009 - Springer
     

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    Protein Summary

    Mouse scavenger mRNA decapping enzyme (DcpS; gi:16740816, Pfam05652) is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' decay of an mRNA (PubMed:16001405). The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. Mouse DcpS contains a histidine triad (HIT) sequence with three histidines (His274, His276, and His278) separated by hydrophobic residues. The central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain. Tyr273 in human DcpS seems to play an important role in cap binding and product release (PubMed:15769464).


    DcpS has two domains: N-terminal domain has mRNA decapping enzyme DcpS N-terminal domain fold (SCOP sunid:102859); C-terminal domain has HIT-like fold (SCOP sunid:54196). Structural neighbours of mouse DcpS found with FATCAT server: 1xmlB, 1xquA, 1av5A, 1y23A, and 1fhi.

    Ligand Summary



    References

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