The Open Protein Structure Annotation Network
PDB Keyword


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

    Title Crystal structure of CT0912, ORFan protein from Chlorobium tepidum with a ferredoxin-like domain repeat (NP_661805.1) from CHLOROBIUM TEPIDUM TLS at 1.80 A resolution. To be published
    Site JCSG
    PDB Id 3gn6 Target Id 390740
    Molecular Characteristics
    Source Chlorobium tepidum tls
    Alias Ids TPS14613,NP_661805.1,, 85631 Molecular Weight 35046.84 Da.
    Residues 320 Isoelectric Point 5.73
    Sequence mtglsqsqaspmqiqpgnaafnpwtdaaldtirdvnqaltlyaemrvvpahhdaflaaidtvsaklrvl pgflslalkqmsgdstmvknypetykgvlatayldgvaagtqpyfynlfvrfadgraaraagfealfet hihpllhamaprggdgpellayravlqsvvagdrhaiyrgaeeirsflrrpvelperetvtvenhvmvp edkhaawepqvaillqvaqdtfepqdepsgvglpgardnryyrkalsteilrnahadgglrayimhgvw esvwdhenshldprflaaagpvgaaavvgpvepfyltrrlvvad
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 4
    Resolution (Å) 1.80 Rfree 0.192
    Matthews' coefficent 2.60 Rfactor 0.163
    Waters 1054 Solvent Content 52.70

    Ligand Information


    Google Scholar output for 3gn6

    Protein Summary

    Chlorobium tepidum tls protein CT0912 (target DB id 390740, accession number NP_661805, gi number 21673740) does not share sequence similarity to any other protein in the public databases, inlcuding other Chlorobium species. The only homolog was found in JGI metagenomic study of uranium contaminated ground water (http://img.jgi.doe.gov/cgi-bin/m/mai...oid=2007105176). Structure of CT0912  consists of a repeat of two similar domains with the ferredoxin-like fold, which is likely a result of gene duplication even though this repeat is not detectable on the sequence level. The N- and C-terminal ferredoxin-like domains are arranged back-to-back to form a barrel and resemble several other proteins of the "dimeric alpha+beta barrel" superfamily of the ferredoxin-like fold of SCOP, with the strongest structural similarity to the sulphur oxygenase reductase, 2cb2. Interestingly, the metal binding site of 2cb2 and CT0912 is located at the opposite half. However, the metal coordination site in CT0912 consists of: His282/His286/Glu308, compared to 2cb2: His86/His90/His114, i.e same residues but different locations. CT0912 does not contain the conserved cysteines essential for 2cb2, the active site is highly hydrophobic and near dimer interface, probably suggesting similar catalytic mechanism but different substrate.



    Figure 1. monomer with Mg as red sphere


    Figure 2. Active site



    >2007105176 [Uranium Contaminated Groundwater FW106]
              Length = 119

     Score = 88.2 bits (217), Expect = 4e-16
     Identities = 44/76 (57%), Positives = 53/76 (69%)

               V   +T YAE+RV+P+    F  A+   + ++R  PGFLS  LKQMSG+STMVKNYPE Y

    Query: 95  KGVLATAYLDGVAAGT 110
               KG LA AYLDGV A T
    Sbjct: 103 KGALANAYLDGVQAHT 118






    Urich, T.,  Gomes, C.M.,  Kletzin, A.,  Frazao, C. (2006) X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme. Science 311: 996-1000

    Ligand Summary




    No references found.

    Files (2)

    FileSizeDateAttached by 
    monomer with mg
    119.38 kB05:19, 5 Mar 2009qxuActions
    active site with red mg
    153.65 kB05:10, 5 Mar 2009qxuActions
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