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The Open Protein Structure Annotation Network
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2fno

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

    Title Comparative structural analysis of a novel glutathioneS-transferase (ATU5508) from Agrobacterium tumefaciens at 2.0 A resolution. Proteins 65 527-537 2006
    Site JCSG
    PDB Id 2fno Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1331,15162326
    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 XRAY
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    Chains 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.67 Rfactor 0.181
    Waters
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    Solvent Content 53.60

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2fno
    1. Comparative structural analysis of a novel glutathioneS_transferase (ATU5508) from Agrobacterium tumefaciens at 2.0 resolution
    M Kosloff, GW Han, S Krishna - PROTEINS: , 2006 - Wiley Online Library
     
    2. A novel structural motif and structural trees for proteins containing it
    AM Kargatov, AV Efimov - Biochemistry (Moscow), 2010 - Springer
     
    3. The role of a conserved interdomain interaction in Escherichia coli Glutaredoxin-2
    N Parbhoo - 2010 - wiredspace.wits.ac.za
     

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    Protein Summary

    The Atu5508 gene from A. tumefaciens encodes the NP_396442 protein, a putative glutathione S-transferase (GST) (PF02798, PF00043). The N-terminal domain of proteins from this family has a thioredoxin fold and is involved in glutathione binding. It is more  conserved than the helical C-terminal domain, forming GST specific fold of a closed 4 helical bundle forming a righ-handed superhelix.

    SCOP classifies 2fno N-terminal domain (1-88) inside the alpha/beta class, thioredoxin-like superfamily, GST N-terminal domain family; and the C-terminal region (88-236) in the all alpha class, GST C-terminal domain like (super)family. 2fno structure is strongly similar (DALI Z-scores) to other glutathione S-transferases, like:

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    (Z=22),
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    (Z=21),
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    (Z=21),
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    (Z=22), despite relatively low sequence identity (~15-20%).

    Analysis of the crystallographic packing of 2fno using the PQS server {Henrick, 1998 #73} indicates that a dimer is the biologically relevant form.

    Ligand Summary



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