1NYR

Structure of Staphylococcus aureus threonyl-tRNA synthetase complexed with ATP


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.313 
  • R-Value Work: 0.239 
  • R-Value Observed: 0.239 

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This is version 1.3 of the entry. See complete history


Literature

Conformational movements and cooperativity upon amino acid, ATP and tRNA binding in threonyl-tRNA synthetase

Torres-Larios, A.Sankaranarayanan, R.Rees, B.Dock-Bregeon, A.C.Moras, D.

(2003) J Mol Biol 331: 201-211

  • DOI: https://doi.org/10.1016/s0022-2836(03)00719-8
  • Primary Citation of Related Structures:  
    1NYQ, 1NYR

  • PubMed Abstract: 

    The crystal structures of threonyl-tRNA synthetase (ThrRS) from Staphylococcus aureus, with ATP and an analogue of threonyl adenylate, are described. Together with the previously determined structures of Escherichia coli ThrRS with different substrates, they allow a comprehensive analysis of the effect of binding of all the substrates: threonine, ATP and tRNA. The tRNA, by inserting its acceptor arm between the N-terminal domain and the catalytic domain, causes a large rotation of the former. Within the catalytic domain, four regions surrounding the active site display significant conformational changes upon binding of the different substrates. The binding of threonine induces the movement of as much as 50 consecutive amino acid residues. The binding of ATP triggers a displacement, as large as 8A at some C(alpha) positions, of a strand-loop-strand region of the core beta-sheet. Two other regions move in a cooperative way upon binding of threonine or ATP: the motif 2 loop, which plays an essential role in the first step of the aminoacylation reaction, and the ordering loop, which closes on the active site cavity when the substrates are in place. The tRNA interacts with all four mobile regions, several residues initially bound to threonine or ATP switching to a position in which they can contact the tRNA. Three such conformational switches could be identified, each of them in a different mobile region. The structural analysis suggests that, while the small substrates can bind in any order, they must be in place before productive tRNA binding can occur.


  • Organizational Affiliation

    Laboratoire de Biologie et Génomique Structurales, IGBMC, 1 rue Laurent Fries, BP 10142, 67400 Illkirch Cedex, France.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
threonyl-tRNA synthetase 1
A, B
645Staphylococcus aureusMutation(s): 0 
EC: 6.1.1.3
UniProt
Find proteins for Q8NW68 (Staphylococcus aureus (strain MW2))
Explore Q8NW68 
Go to UniProtKB:  Q8NW68
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8NW68
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.313 
  • R-Value Work: 0.239 
  • R-Value Observed: 0.239 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 104.13α = 90
b = 122.521β = 90
c = 148.661γ = 90
Software Package:
Software NamePurpose
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-10-28
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-16
    Changes: Data collection, Database references, Derived calculations, Refinement description