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The Open Protein Structure Annotation Network
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3ohg

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

    Title Crystal structure of a protein with unknown function from DUF2233 family (BACOVA_00430) from Bacteroides ovatus at 1.80 A resolution. To be published
    Site JCSG
    PDB Id 3ohg Target Id 416706
    Molecular Characteristics
    Source Bacteroides ovatus atcc 8483
    Alias Ids TPS33812,ZP_02063482.1, 384454 Molecular Weight 31070.58 Da.
    Residues 284 Isoelectric Point 5.39
    Sequence mpqtaigrqlvesgmandvtldnesvvrdgiklnelafktfgesqhifvatidlneltftpatkddknv patgpessaplpihafaaeangktvwlgvngdyyadnprrvmglfykdgvcinsqyfeghdevlyqlkn getyvgqadealaheanllhalggygllvkdgvvqnfyeemgdlqnthprtsvglsqdrktmyvfvvdg rrkdsffalgltlphlatmmkavgcynainldgggsttliirkvndggkptfpilntpaddrvprkvtn smliiekk
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.80 Rfree 0.1507
    Matthews' coefficent 3.92 Rfactor 0.1291
    Waters 487 Solvent Content 68.63

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 3ohg

    Protein Summary

    Pfam update: This protein is a member of the DUF2233 (PF09992) family, described as putative periplasmic proteins  with unknown function and structure. This family is broadly distributed in Bacteria and Eukaryots, but not in Archea. Its mammalian homologs seem to have solid experimental based function of N-acetylglucosamine-1-phosphodiester �dc03-N-acetylglucosaminidase (“uncovering enzyme” or UCE or “Nagpa”), which is involved in converting mannose 6-phosphate (Man-6-P) diesters to Man-6-P monoesters [Ref]. Apparently based on this annotation, JGI calls proteins from this family "Exopolysaccharide biosynthesis proteins" but as far as I can tell no bacterial homolog have been directly studied.

    This protein appears to be a lipoprotein as it has a predicted SpII cleavage site.

    It has the Uniprot id A7LRK2 (A7LRK2_BACOV) and has been assigned to Pfam PF09992/DUF2233.

    It is annotated as a protein of unknown function. According to Pfam, there are 494 unique proteins in this family from 184 species that contain the DUF2233 domain as part of proteins up to ~1000 residues and they are observed in 34 architectures.

    It is present as a monomer in the crystal structure. PISA analysis suggests that a monomer is the preferred oligomeric form in solution.

    FFAS did not yield any structural prediction for this family.

    A search against the Conserved Domain Database produces hits to EpsL and DUF2233 family and PSI-BLAST shows hits to some proteins annotated as N-acetylmuramoyl-L-alanine amidase (AmiD).

    Through a FATCAT search, the N-terminal domain has some similarity to human latexin (PDB id 2bo9) that is the endogenous inhibitor of metallocarboxypeptidase.

    A DALI search results in numerous hits with Z-score > 4.5, for example with PDB ids 2obd (cholesteryl ester transfer protein), 2p4b (sigma E regulatory protein RSEB, and 2qfm (spermine synthase). The hits match to some portions of this target.

    Further analysis has been performed.

    A manuscript is almost complete on this structure and the human homolog.

    Fig1.png

    Ligand Summary

    Reviews

    References

     

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