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The Open Protein Structure Annotation Network
PDB Keyword
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387040

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

    Site JCSG
    Status Diffraction-quality Crystals
    Target Id 387040
    Molecular Characteristics
    Source Ralstonia eutropha jmp134
    Alias Ids TPS7478, Molecular Weight 40246.73 Da.
    Residues 358 Isoelectric Point 5.90
    Sequence mssnvshfegtrpvadqqrfdtealeawmrqhvegfagplsveqfkggqsnptfklvtpgqtyvmrakpgpkskll psahaiereyrvmdalagtdvpvakmyalcedesvigrafyimefvsgrvlwdqslpgmspaertaiydemnrvi aamhtvdyqaiglgdygkpgnyfqrqierwtkqyklsetesipamdslmdwlpqhipqedadltsivhgdyrldn lmfhpteprvlavldwelstlghpmgdfgyhcmswhiapgqfrgiagldhaalgipdeasyrklyeqrtgrpitg dwnfylafsmfriagilqgimkrvvdgtassaqaldagkrarpmaemgweyakkakq
      BLAST   FFAS
    Ligand Information
    Ligands
    Metals
    Google Scholar output for

    Protein Summary

    Member of the CAK family of small molecule kinases, within the protein kinase-like (PKL) fold.

    The Sequence matches out APH domain (http://pfam.sanger.ac.uk/family?id=APH.  Residues D221 is expected to be the active site residue. -- Rob Finn, PFAM.

    There is a protomer (blue) in the assymetric unit of the  unit cell of the crystal lattice, but crystal structure packing analysis suggests that the favored oligomeric form in solution should be a dimer (blue and red):

    EK5976M_Fig1.pngThis family is widespread in proteobacteria, where one genome may have multiple copies. A very similar domain is found in most eukaryotic organisms (e.g. ACAD10, ACAD11 in human), where it is fused to acyl CoA dehydrogenase domains. The significance of this linkage is reflected by this protein frequently sharing an operon with acyl CoA dehydrogenase domains in bacteria.

    The key catalytic motifs are conserved in this protein, and the family is largely typical of other CAKs, though with a characteristic catalytic loop sequence (HGDYRLDN, yellow) where the Y is almost unique, and the R is in the place of the K within the serine/threonine kinase catalytic loop:


    EK5976M_Fig2CatalyticLoop.png

     

     

    A superimpostion of this crystal structure with that of the other JCSG "EK" targets (3csv.pdb, cyan, Crystal structure of a putative aminoglycoside phosphotransferase (YP_614837.1) from Silicibacter sp. TM1040; 3d1u.pdb, magenta, Crystal structure of putative fructosamine-3-kinase (YP_290396.1) from Thermobifida fusca  YX-ER1 at 1.85 A resolution; and EK14125A, yellow, Mll5367 protein from Mesorhizobium loti) reveals their overall structural similarity but differences in the details:

    EK5976M_Fig3Comparisons.png

    Ligand Summary

    Reviews

    References

     

    No references found.

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    Files (3)

    FileSizeDateAttached by 
     EK5976M_Fig1.png
    Dimer
    332.13 kB21:38, 21 Jul 2008debanuActions
    EK5976M_Fig2CatalyticLoop.png
    Catalytic Loop Sequence
    345.53 kB21:56, 21 Jul 2008debanuActions
     EK5976M_Fig3Comparisons.png
    Superimposition with other JCSG "EK" target structures
    691.11 kB21:46, 21 Jul 2008debanuActions
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