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2kl4

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

    Title Solution structure of the protein NB7804A from Bacillus Halodurans. To be Published
    Site JCSG
    PDB Id 2kl4 Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS29794,NP_242898.1, BIG_439, BIG_25
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method NMR
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    Chains 1

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2kl4

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    Protein Summary

    The gene BH2032 (NP_242898) from Bacillus halodurans encodes the protein from the PFAM DUF1801 PF08818 family.  Several other proteins from this family were solved by other SG centers (JCSG - 2oc6, 2i8d). The DUF1801 family consists of over 600 mostly bacterial proteins with unknown functions (single homologs are also found in archea, viruses. The only eukaryotic homolog is found in Trichomonas vaginalis, an anaerobic parasitic protozoan, source of very common but mostly asymptomatic STD)   

    2kl4 structure is assigned to the YdhG-like (super)family (SCOP159889). DALI conforms similarity to other members of this family, but also a marginal similarity to NADH-quinone oxidoreductase subunit-1 3iam (Z=6) and to proteins from the bacterial frataxin family (2EFF; Z=5.5).

    Another recent report suggests that although YdhG proteins lack detectable sequence similarity, the structural and functional similarity to the bacterial frataxin family (2EFF; Z=5.5) suggests their general role as frataxin-type proteins in iron homeostasis [Ref].  The function of frataxin is not entirely clear, but it seems to be involved in assembly of iron-sulfur clusters. It has been proposed to act as either an iron chaperone or an iron storage protein [Ref].

     
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    2fki and 2aiv belong to DUF419 (PF04237)

    Analysis of the E.coli homolog (2fki) suggested a possible DNA binding activity for proteins from this family (Singarapu KKLiu GXiao RBertonati CHonig BMontelione GTSzyperski T. NMR structure of protein yjbR from Escherichia coli reveals 'double-wing' DNA binding motif. Proteins. 2007 May 1;67(2):501-4.), but the analysis presented in this paper is not entirely convincing.

    Ligand Summary

    Reviews

    References

     

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