The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of hypothetical protein (NP_953832.1) from Geobacter sulfurreducens at 1.50 A resolution. To be published
    Site JCSG
    PDB Id 2opl Target Id 371567
    Molecular Characteristics
    Source Geobacter sulfurreducens pca
    Alias Ids TPS1584,NP_953832.1, 91101 Molecular Weight 20432.29 Da.
    Residues 186 Isoelectric Point 5.26
    Sequence msqttvvngvnvdqlmatieqikakpeiaqfkfratnqwmggthnqatikdfygacaeddtrkpmvfdl deppvllgenrganpveyllvalsgclttslvahaaargialrgvksryegdidlrgflglseevpvgy reirvffsidadltdgqkeelirmaqkyspvyntvakpvpvavlldrg
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.50 Rfree 0.168
    Matthews' coefficent 2.25 Rfactor 0.15
    Waters 498 Solvent Content 45.39

    Ligand Information


    Google Scholar output for 2opl
    1. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard
    TC Terwilliger, PD Adams, RJ Read - Section D: Biological , 2009 - scripts.iucr.org
    2. The crystal structure of the AF2331 protein from Archaeoglobus fulgidus DSM 4304 forms an unusual interdigitated dimer with a new type of _+ _ fold
    S Wang, O Kirillova, M Chruszcz, D Gront - Protein , 2009 - Wiley Online Library
    3. Widespread Disulfide Bonding in Proteins from Thermophilic Archaea
    J Julien, Y Todd O - Archaea, 2011 - hindawi.com

    Protein Summary

    The gene GSU2788 from Geobacter sulfurreducens encodes the NP_953832 protein, a member of the OsmC family PF02566.  The 2opl structure belongs to the class of alpha and beta (a+b) proteins and adopts an OsmC-like fold type SCOP82783.  DALI hits are with the OsmC-like protein {{note.link("similar", "PDB:1lql )}} (Z=12), TA0195 protein {{note.link("similar", "PDB:2onf")}} (Z=11), and AQ_1549 protein {{note.link("similar", "PDB:2egt")}} (Z=11).

    The OsmC protein functions as a hydroperoxide resistance protein. The osmotically inducible protein OsmC is a member of a family of bacterial proteins involved in the detoxification of organic hydroperoxides.  The organic hydroperoxides are produced during bacterial aerobic respiration, as well as by the host immune system cells as a defense mechanism against the infectious bacteria. OsmC proteins share no sequence homology to other prokaryotic or eukaryotic proteins.  

    The biological unit of the 2opl structure is a homodimer.  The C-terminal domain of the enzyme contains two conserved cysteine residues, which are essential for the catalytic activity of the enzyme: 1) Cys56-S(-) + ROOH --> Cys56-S-OH + ROH; 2) Cys56-S-OH + Cys95 - SH --> Cys56-SS-Cys95 + H2O; 3) Cys56-SS-Cys95 + R(SH)2 --> Cys56-S(-) + Cys95-SH.  [Ref]  

    The structures of the enzyme homologues from other organisms are available: PDB:3cje, Jannaschia; PDB:1vls, Thermotoga maritima; PDB:1nyeE. coli

    Ligand Summary





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