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The Open Protein Structure Annotation Network
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3csw

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

    Title Crystal structure of a Putative Branched-Chain Amino Acid Aminotransferase (TM0831) from Thermotoga maritima at 2.15 A resolution. To be published
    Site JCSG
    PDB Id 3csw Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1240,TM0831, _0012.001391_, _0114.000064_, 84893
    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 4
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 3.98 Rfactor 0.167
    Waters
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    Solvent Content 69.11

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 3csw
    1. Structural analysis of mycobacterial branched-chain aminotransferase: implications for inhibitor design
    A Castell, C Mille, T Unge - Acta Crystallographica Section D: , 2010 - scripts.iucr.org
     

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    Protein Summary

    TM0831 is a putative BACT (branched-chain amino acid aminotransferase, EC 2.6.1.42). It is involved in biosynthesis of valine and isoleucine by catalyzing the following reaction:

    L-LEUCINE + 2-OXOGLUTARATE = 4-METHYL-2-OXOPENTANOATE + L-GLUTAMATE.

    It shared <=30% sequence identity with several BACTs which has been characterized biochemically and structurally (1i1k/1i1l/1i1m; 1iyd/1iye; 1a3g, 1daa, 1g2w, 1wrv). TM0830 functions as a tetramer, in comparison to trimers or monomers in structural homologs. Additionally, it is interesting to note that the PLPs are only present in the A/C active site, but not in B/D. The residues near PLP are strictly conserved (H47, R50, T228, K133, E164, G190, T192). In TM0831 structure, K133 is not covalently linked to PLP. An interesting obvervation is that the helix equivalent to TM0831 helix 138-147 are likely important functionally in BACT, since it is close to the active site and shows larger variations among homologs.



    Despite relative high sequence similarity, the structure differences are larger than expected.

    Structure comparison table (DaliLite results from server http://www.procksi.net/):

    Z-Scores
    StructuresmonaA-11i1kA-11iydA-11a3gA-11daaA-11g2wA-11wrvA-1
    monaA-148.1 # # # # # #
    1i1kA-131.750.9 # # # # #
    1iydA-132.147.353.5 # # # #
    1a3gA-130.646.545.250.2 # # #
    1daaA-130.034.635.133.447.3 # #
    1g2wA-130.035.035.633.744.647.9 #
    1wrvA-131.041.140.940.033.534.051.5

    Number of Alignments
    StructuresmonaA-11i1kA-11iydA-11a3gA-11daaA-11g2wA-11wrvA-1
    monaA-1274 # # # # # #
    1i1kA-1267298 # # # # #
    1iydA-1272297304 # # # #
    1a3gA-1262295294295 # # #
    1daaA-1258271276267277 # #
    1g2wA-1258270275267277277 #
    1wrvA-1268293293291268268297
    RMSD Values
    StructuresmonaA-11i1kA-11iydA-11a3gA-11daaA-11g2wA-11wrvA-1
    monaA-10.0 # # # # # #
    1i1kA-12.10.0 # # # # #
    1iydA-12.10.40.0 # # # #
    1a3gA-12.00.40.60.0 # # #
    1daaA-12.11.41.61.40.0 # #
    1g2wA-12.11.41.51.40.50.0 #
    1wrvA-12.21.11.21.21.41.40.0

    Ligand Summary



    References

    Reviews

    References

     

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