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1o1y

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

    Title Crystal structure of a putative glutamine amido transferase (TM1158) from Thermotoga maritima at 1.7 A resolution. PROTEINS 54 801-805 2004
    Site JCSG
    PDB Id 1o1y Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1266,TM1158, 89436
    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 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.54 Rfactor 0.14516
    Waters
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    Solvent Content 51.21

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1o1y
    1. Finding functional sites in structural genomics proteins
    A Stark, A Shkumatov, RB Russell - Structure, 2004 - Elsevier
     
    2. 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
     
    3. Efficient recognition of protein fold at low sequence identity by conservative application of Psi_BLAST: validation
    FJ Stevens - Journal of Molecular Recognition, 2005 - Wiley Online Library
     
    4. Crystal structure of homoserine O_succinyltransferase from Bacillus cereus at 2.4 resolution
    C Zubieta, S Krishna, D McMullan - Proteins: Structure, , 2007 - Wiley Online Library
     
    5. Crystal structure of a putative glutamine amido transferase (TM1158) from Thermotoga maritima at 1.7 resolution
    R Schwarzenbacher, AM Deacon - Proteins: Structure, , 2004 - Wiley Online Library
     

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    Protein Summary

    The putative glutamine amido transferase (TM1158; NP_228964) from Thermotoga maritima belongs to a group of proteins present in all kingdoms of Life, having the type 1 glutamine amidotransferase (GATase1) domain with Cys88-His173-Glu175 catalytic triad in the glutaminase active site  (Pfam00117, cd01741). Glutamine amidotransferases transfer the amide nitrogen of glutamine to a variety of substrates (PubMed:9559052). The reaction is carried out by glutaminase and synthase subunits from the same or separate polypeptide chains (PubMed:8366040).

    The 1o1y structure of glutaminase subunit (PubMed:14997577) described here, has a flavodoxin-like fold (SCOP sunid: 52171) with 3 layers, alpha/beta/alpha parallel beta-sheet of 5 strands, order 21345. TM1158 belongs to class I glutamine amidotransferases family (GAT; SCOP sunid: 52318).

    Several proteins with structure similar to TM1158 have significant sequence similarity and contain all three catalytic residues (i.e. PDB structures:

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    [Z=29],
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    , chain A [Z=20],
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    , chain A [Z=20],
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    , chain B [Z=21],
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    , chain B [Z=21],
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    , chain A [Z=20],
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    , chain B,
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    , chain A,
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    , chain A,
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    , chain A,
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    , chain H,
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    , chain A,
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    , chain A,
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    , chain A,
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    , chain A,
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    , chain B, 1vcmA ,
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    , chain A).  However TM1158 contains an additional alpha-helical "hairpin" close to the C-terminus (residues 176-210).

    Ligand Summary



    References

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