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

    Title Crystal structure of a bsmA homolog (Mpe_A2762) from Methylobium petroleophilum PM1 at 1.91 A resolution. To be published
    Site JCSG
    PDB Id 3pl0 Target Id 392100
    Molecular Characteristics
    Source Methylibium petroleiphilum pm1
    Alias Ids TPS26547,YP_001021951.1, 325753 Molecular Weight 28222.74 Da.
    Residues 253 Isoelectric Point 5.81
    Sequence mhvdielplgratalqrlraqgfcvltpaaletltgmpldafdmmlpyweelapdlhlkdgghyryrrh gcfmqtlqpgqletvqhrahwqpttynalhggmerwfeplsnemihlpswsallvalgelfaklrapqg grwyieahpfridteggvgrptpegahrdgvdfvavvfigrqgvrggetrvfdaagpqgvrftleqpwt vlllddqqvihestpllpldpadpavpahrdtlvltyrsggfqapa
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.91 Rfree 0.2109
    Matthews' coefficent 2.49 Rfactor 0.1694
    Waters 419 Solvent Content 50.50

    Ligand Information


    Google Scholar output for 3pl0

    Protein Summary

    This protein is a homolog of BsmA, which is involved in quorum sensing-controlled biofilm development in
    Serratia liquefaciens MG1.The exact function is unknown. This protein could be an enzyme or substrate-binding protein. A large, well-defined, conserved cavity is located on the protein surface (Fig2). 


    This is the first structure of family DUF2257. The structure reveals that this family are novel dioxygenases. Active site residues for this protein: His165, Asp167, His218. Based on similarity to other proteins, this protein would bind Fe2+ and 2OG (2-oxoglutarate). As a result, this family can be assigned a member of  2OG-FeII_Oxy (PF03171), even though sequence similarity is only restricted to catalytic residues.


    Potential residues for substrate specificity: Arg65 (c=conserved), Arg104 (c), Arg67 (c), His89,Gln91 (c), Phe106 (c), His146 (c), Phe148 (hydrophobic), Val241 (hydrophobic), Thr243.


     Fig. 1. monomer



    Fig. 2. surface


    From Pfam:

    This sequence matches family DUF2257 (PF10014), for which there are no other structures.

    From Krishna:

    This protein shares remote sequence similarity with the
    Double-stranded beta-helix fold of SCOP and should be classified as
    such ( http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.c.bdi.A.html ).
    In addition, there is also reasonable similarity with DUF2086
    (PF09859) and the CsiD family of non-heme Fe(II)-dependent
    oxygenase(PF08943). Therefore both DUF2086 and DUF2257 should be
    included as members of the Cupin clan of Pfam.

    Ligand Summary




    No references found.

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    Files (2)

    FileSizeDateAttached by 
    surface of fr14672c
    210.87 kB19:37, 22 Sep 2010qxuActions
    137.78 kB19:35, 22 Sep 2010qxuActions
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