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The Open Protein Structure Annotation Network
PDB Keyword
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2qyc

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

    Title Crystal structure of dimeric ferredoxin-like protein (NP_888056.1) from Bordetella bronchiseptica at 1.90 A resolution. To be published
    Site JCSG
    PDB Id 2qyc Target Id 378277
    Molecular Characteristics
    Source Bordetella bronchiseptica rb50
    Alias Ids TPS1718,NP_888056.1, 3.30.70.900, 103982 Molecular Weight 11322.42 Da.
    Residues 102 Isoelectric Point 5.61
    Sequence mtmflhvvmmefddgidagffrtvdeyvarmkrecdglllyhfgenvaarsqgythatssafvdaaahd ayqvcpahvamkafmgprikrvvvydgevpaig
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.90 Rfree 0.236
    Matthews' coefficent 2.34 Rfactor 0.177
    Waters 120 Solvent Content 47.48

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2qyc

    Protein Summary

    Gene BB1511 from Bordetella bronchiseptica encodes the NP_888056 protein that belongs to the Dabb family (Stress responsive A/B Barrel Domain) PF07876. This protein is also related to BB0372 (35% seq.id.) of unknown function.

    2qyc has an alpha+beta structure that adopts a ferredoxin-like fold, inside the dimeric alpha+beta barrel superfamily, plant stress induced protein family of SCOP. According to a DALI search, 2qyc shows structural similarity to plant stress-induced proteins, namely the boiling stable protein (PDB:1tr0; Z=14, 19% sequence identity) from Populus tremula and proteins AT3G17210.1 (PDB:1q4r, PDB:1q53; Z=13-11) and AT5G22580 (PDB:1rjj; Z=11) from Arabidopsis thaliana. The smallest stable unit of all these beta-barrel plant proteins is a dimer, which is further packed in higher-order oligomers. Interestingly 2qyc crystallizes as a dimer but does not form higher-order oligomers. Furthermore, the dimer interface is not conserved when compared to the boiling stable protein 1tr0 [Ref] where residues Lys-10, Glu-68, Tyr-105 participate in an extensive hydrogen bonding and salt bridge network across different copies of the protein chains. 

    Ligand Summary



    References

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