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The Open Protein Structure Annotation Network
PDB Keyword
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2avn

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

    Title Crystal structure of Ubiquinone/menaquinone biosynthesis methyltransferase-related protein (tm1389) from THERMOTOGA MARITIMA at 2.35 A resolution. To be published
    Site JCSG
    PDB Id 2avn Target Id 283250
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1283,TM1389, 89953, 90017 Molecular Weight 28809.44 Da.
    Residues 248 Isoelectric Point 5.16
    Sequence mklrswefydriaraydsmyetpkwklyhrligsfleeylknpcrvldlgggtgkwslflqergfevvl vdpskemlevarekgvknvveakaedlpfpsgafeavlalgdvlsyvenkdkafseirrvlvpdgllia tvdnfytflqqmiekdawdqitrflktqttsvgttlfsfnsyafkpedldslegfetvdirgigvmeyp derisereetifrleqelsrdrniiwkadhiffvlkkkrga
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.35 Rfree 0.199
    Matthews' coefficent 3.96 Rfactor 0.169
    Waters 210 Solvent Content 68.67

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2avn
    1. Bud23 methylates G1575 of 18S rRNA and is required for efficient nuclear export of pre-40S subunits
    J White, Z Li, R Sardana, JM Bujnicki - and cellular biology, 2008 - Am Soc Microbiol
     
    2. A Conformational Switch in the Active Site of BT_2972, a Methyltransferase from an Antibiotic Resistant Pathogen B. thetaiotaomicron
    V Kumar, J Sivaraman - PloS one, 2011 - dx.plos.org
     

    Protein Summary

    The gene TM1389 from Thermotoga maritima encodes ubiquinone/menaquinone biosynthesis methyltransferase class I, most probably 3-demethylubiquinone-9 3-O-methyltransferase [Ref] E.C.2.1.1.64.  The enzyme contains methyltransferase domain, which belongs to a family of S-adenosyl-L-methionine-dependent methyltransferases (SAM or AdoMet-MTase) PF08241 COG0684.  The enzyme uses S-adenosyl-L-methionine as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class, enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).

    Ligand Summary



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