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The Open Protein Structure Annotation Network
PDB Keyword
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2qs7

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

    Title Crystal structure of protein of unknown function (NP_342590.1) from Sulfolobus solfataricus at 2.09 A resolution. To be published
    Site JCSG
    PDB Id 2qs7 Target Id 372180
    Molecular Characteristics
    Source Sulfolobus solfataricus p2
    Alias Ids TPS1602,NP_342590.1, BIG_508, 103447 Molecular Weight 16110.99 Da.
    Residues 143 Isoelectric Point 5.45
    Sequence maeekkkklsiivfsgtidklmpvgiltsgaaasgyevnlfftfwglqaitkrslnsqqppqidknyeq mgpimmqkmqemkypmwhqlvqqakeigevkvfacsttmeffgikredlaefvddvvgvatfldraegg ttlfi
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 4
    Resolution (Å) 2.09 Rfree 0.203
    Matthews' coefficent 2.68 Rfactor 0.176
    Waters 85 Solvent Content 54.13

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2qs7

    Protein Summary

    Gene SSO1126 from Sulfolobus solfataricus translates into the NP_342590 amino acid sequence that belongs to the DsrE/DsrF-like group (PF02635).

    Pre-SCOP classifies 2qs7 in the alpha/beta class, DsrEFH-like superfamily, DsrEF-like family. DALI top hits for a search with 2qs7 are with uncharacterized protein 1l1s (Z=14), YCHN protein 1jx7 (Z=13), STO148 protein 2pd2 (Z=12) and a putative DSRE protein 2hy5 (Z=12). 2qs7 folds into a structure similar (rmsd 2.3 Å over 100 residues, 13% sequence id, Z=12) to 2fb6 from Bacteroides thetaiotaomicron, a member of the human gut microbiome.

        

    PF02635 family (example structure PDB id: 1l1s) exhibits structural similarity to dehydrogenases, amidohydrolases and oxidoreductases. Sequence and structural analyses have shown that 2qs7 does not belong to the dehydrogenase or the amidohydrolase superfamilies of proteins ([Ref]). Psi-BLAST run gives high probability of SSO1126 functioning as an NADH dehydrogenase (EC 1.6.99.3) or as an FAD-dependent pyridine nucleotide-disulphide oxidoreductase (EC 1) with respective E values of 1e-38 and 2e-38. The redox role for SSO1126 is further supported by the domain organization of other family members and genomic context of SSO1126 which includes other redox subunits and proteins (SSO1127: heterodisulfite reductase, subunit C; SSO1129: heterodisulfite reductase, subunit B; SSO1123: dihydrolipoamide dehydrogenase).

     

    To do: more refined structural comparisons with the above oxidoreductases, and the three relevant structures (2qs7, 2fb6, 1l1s). Also,  look at bound ligand (piperazine); this may help locate the co-factor (NAD or FAD) binding site.

    Ligand Summary


    References

    Reviews

    References

     

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