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    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 283024
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1266,TM1158, 89436 Molecular Weight 26898.77 Da.
    Residues 227 Isoelectric Point 5.66
    Sequence mrvlairhveiedlgmmedifreknwsfdyldtpkgeklerpleeyslvvllggymgayeeekypflky efqlieeilkkeipflgiclgsqmlakvlgasvyrgkngeeigwyfvekvsdnkffrefpdrlrvfqwh gdtfdlprratrvftsekyenqgfvygkavglqfhievgartmkrwieaykdelekkkidprllletae reekvlkgllrsllermves
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.70 Rfree 0.17242
    Matthews' coefficent 2.54 Rfactor 0.14516
    Waters 358 Solvent Content 51.21

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    Ligand Information


    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

    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: PDB:3l83 [Z=29], PDB:2a9v, chain A [Z=20], PDB:1wl8, chain A [Z=20], PDB:1qdl, chain B [Z=21], PDB:1i7q, chain B [Z=21], PDB:2h2w, chain A [Z=20], PDB:1i1q, chain B, PDB:1kxj, chain A, PDB:1q7r, chain A, PDB:1r9g, chain A, PDB:1ka9, chain H, PDB:1l9x, chain A, PDB:1gpm, chain A, PDB:1jvn, chain A, PDB:2abw, chain A, PDB:1bxr, chain B, 1vcmA , PDB:1s1m, chain A).  However TM1158 contains an additional alpha-helical "hairpin" close to the C-terminus (residues 176-210).

    Ligand Summary





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