.
The Open Protein Structure Annotation Network
PDB Keyword
.

2g36

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

    Title Structure of a tryptophanyl-tRNA synthetase containing an iron-sulfur cluster. Acta Crystallogr.,Sect.F 66 1326-1334 2010
    Site JCSG
    PDB Id 2g36 Target Id 282365
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1210,TM0492, 89386 Molecular Weight 37767.59 Da.
    Residues 328 Isoelectric Point 5.86
    Sequence mrilsgmrptgklhighlvgalenwvklqeegnecfyfvadwhaltthyddvsklkeytrdlvrgflac gidpeksvifvqsgvkehaelallfsmivsvsrlervptykeikselnykdlstagfliypvlqaadil iykaegvpvgedqvyhieltreiarrfnylydevfpepeailsrvpklpgtdgrkmsksygniinleis ekeleqtilrmmtdparvrrsdpgnpencpvwkyhqafdiseeeskwvwegcttasigcvdckklllkn mkrklapiwenfrkidedphyvddvimegtkkarevaaktmeevrramnlmf
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.50 Rfree 0.256
    Matthews' coefficent 3.37 Rfactor 0.194
    Waters 56 Solvent Content 63.17

    Pathway

    Reactions found in Metabolic Reconstruction for TM0492

    Name: Tryptophanyl-tRNA synthetase
    Metabolic Subsystem: tRNA Metabolism
    Reaction: : atp + trnatrp + trp-L --> amp + ppi + trptrna
    Classification: EC:6.1.1.2
     

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2g36
    1. Ironsulfur protein folds, ironsulfur chemistry, and evolution
    J Meyer - Journal of Biological Inorganic Chemistry, 2008 - Springer
     
    2. Phylogeny and molecular signatures for the phylum Thermotogae and its subgroups
    RS Gupta, V Bhandari - Antonie van Leeuwenhoek, 2011 - Springer
     
    3. De novo design of a non-natural fold for an iron-sulfur protein: Alpha-helical coiled-coil with a four-iron four-sulfur cluster binding site in its central core
    J Grzyb, F Xu, L Weiner, EJ Reijerse, W Lubitz - et Biophysica Acta (BBA , 2010 - Elsevier
     
    4. Crystal structure of Pyrococcus horikoshii tryptophanyl-tRNA synthetase and structure-based phylogenetic analysis suggest an archaeal origin of tryptophanyl-tRNA
    X Dong, M Zhou, C Zhong, B Yang, N Shen - Nucleic acids , 2010 - Oxford Univ Press
     
    5. Structure of a tryptophanyl-tRNA synthetase containing an iron-sulfur cluster
    GW Han, XL Yang, D McMullan, YE Chong - Section F: Structural , 2010 - scripts.iucr.org
     
    6. STREPTAVIDIN MACROMOLECULAR ADAPTOR AND COMPLEXES THEREOF
    FR Salemme, PC Weber - US Patent App. 12/766,658, 2010 - Google Patents
     
    7. The development and application of methods to study the evolution of specificity, allostery, and RNA-protein interactions in translation
    A Sethi - 2008 - books.google.com
     

    Protein Summary

    The hyperthermophilic bacterium Thermotoga maritima has been the target of choice at the JointCenter for Structural Genomics (JCSG) for pipeline development and genome-wide structural annotation. Aminoacyl tRNA-synthetases (AARSs) are important enzymes of the protein translation apparatus. They are present in organisms from all kingdoms of life and are considered central to the origin of life. The main function of these proteins are to covalently append the 20 standard amino acids to their cognate tRNA's. The reaction proceeds in a two-step ATP-dependent manner, with the amino acid activated by its interaction with ATP in the first step. In the subsequent step, the mixed-anhydride reacts with tRNA forming an aminoacyl-tRNA. Most organisms contain individual tRNA-synthetases specific towards each of the twenty standard amino acids. Based on similarities in their sequences and structures, aaRSs have been broadly grouped into two classes (class I and II) each containing 10 aaRSs. Tryptophanyl tRNA-synthetase (E.C 6.1.1.2) is a class I aaRS. Members of this class typically adopt a Rossmann fold and contain two highly conserved sequence motifs "HIGH" and "KMSKS" that are critical for function. Apart from TrpRS the class I group also contains ArgRS, CysRS, GlnRS, GluRS, IleRS, LeuRS, MetRS, ValRS, and TyrRS. Among these, TyrRS is particularly close, both in terms of sequence and structural similarity, to TrpRS .
    Similar to the structures of other TrpRSs, TM0492 consists of two domains. The N-terminal catalytic domain adopts a canonical Rossmann fold (RF; residues 1-181, 295-328) with a central five-stranded parallel b-sheet (b1- b5, strand order for the b-sheet is 32145), and the TAB domain adopts an all-helical fold (residues 187-285). The C-terminal TAB domain is composed of five helices (H12-H16) that are packed as a bundle. In addition, a short hinge region (182-186) connects the RF and the TAB domains. The catalytic domain of TrpRSs belong to the nucleotidylyl transferase superfamily of SCOP.


    Ligand Summary

    TM0492 has a [4Fe-4S] cluster bound at the C-terminal tRNA anti-codon binding (TAB) domain, and a L-Trp molecule bound at the active site. In addition, the final model contains two chlorine ions and 56 water molecules.
    TM0492 is the first aaRS
    structure in which a [4Fe-4S] cluster is seen bound at the TAB domain, close to the anticodon binding site.


    References

    Reviews

    References

     

    No references found.

    Tag page

    Files (0)

     
    You must login to post a comment.
    All content on this site is licensed under a Creative Commons Attribution 3.0 License
    Powered by MindTouch