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1o5i

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

    Title Crystal structure of 3-oxoacyl-(acyl carrier protein) reductase (TM1169) from Thermotoga maritima at 2.50 A resolution. To be published
    Site JCSG
    PDB Id 1o5i Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1267,TM1169, 84740
    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 2.54 Rfactor 0.19404
    Waters
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    Solvent Content 51.23

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1o5i
    1. Allosteric disulfide bonds
    B Schmidt, L Ho, PJ Hogg - Biochemistry, 2006 - ACS Publications
     
    2. The importance of alignment accuracy for molecular replacement
    R Schwarzenbacher, A Godzik - Section D: Biological , 2004 - scripts.iucr.org
     
    3. Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity
    TP Korman, JA Hill, TN Vu, SC Tsai - Biochemistry, 2004 - ACS Publications
     
    4. Shotgun crystallization strategy for structural genomics II: crystallization conditions that produce high resolution structures for T. maritima proteins
    R Page, AM Deacon, SA Lesley - Journal of structural and , 2005 - Springer
     
    5. Structure/function of human type 1 3 [beta]-hydroxysteroid dehydrogenase: An intrasubunit disulfide bond in the Rossmann-fold domain and a Cys residue in the
    JL Thomas, R Huether, VL Mack, LA Scaccia - The Journal of steroid , 2007 - Elsevier
     
    6. A unique catalytic triad revealed by the crystal structure of APE0912, a short_chain dehydrogenase/reductase family protein from Aeropyrum pernix K1
    A Yamamura, T Ichimura, F Mimoto - Proteins: Structure, , 2008 - Wiley Online Library
     
    7. Divergent evolution of a Rossmann fold and identification of its oldest surviving ancestor
    WL Duax, R Huether, V Pletnev - International journal of , 2009 - Inderscience
     
    8. Crystallization of an atypical short-chain dehydrogenase from Vibrio vulnificus lacking the conserved catalytic tetrad
    G Buysschaert, K Verstraete, SN Savvides - Section F: Structural , 2012 - scripts.iucr.org
     

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    Protein Summary

    The gene TM1169 from Thermotoga maritima encodes 3-oxoacyl-(acyl carrier protein) fabG reductase EC:1.1.1.212.  The enzyme belongs to a superfamily of Rossmann-fold NAD(P)(+)-binding proteins COG4982.  This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in fatty acid biosynthesis and polyunsaturated fatty acid biosynthesis.  Dozens of  structures have been solved for this class of enzymes, e.g 3FDA from Rickettsia Prowazekii.  The amino acid sequence of this protein is highly identical (99%) to a short-chain dehydrogenase/reductase SDR PF00106 from Thermotoga petrophila.  It is possible that this enzyme has a rather broad substrate specificity.

    Ligand Summary



    References

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