1KOG

Crystal structure of E. coli threonyl-tRNA synthetase interacting with the essential domain of its mRNA operator


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.287 
  • R-Value Work: 0.251 
  • R-Value Observed: 0.251 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Structural basis of translational control by Escherichia coli threonyl tRNA synthetase.

Torres-Larios, A.Dock-Bregeon, A.C.Romby, P.Rees, B.Sankaranarayanan, R.Caillet, J.Springer, M.Ehresmann, C.Ehresmann, B.Moras, D.

(2002) Nat Struct Biol 9: 343-347

  • DOI: https://doi.org/10.1038/nsb789
  • Primary Citation of Related Structures:  
    1KOG

  • PubMed Abstract: 

    Escherichia coli threonyl-tRNA synthetase (ThrRS) represses the translation of its own messenger RNA by binding to an operator located upstream of the initiation codon. The crystal structure of the complex between the core of ThrRS and the essential domain of the operator shows that the mRNA uses the recognition mode of the tRNA anticodon loop to initiate binding. The final positioning of the operator, upon which the control mechanism is based, relies on a characteristic RNA motif adapted to the enzyme surface. The finding of other thrS operators that have this conserved motif leads to a generalization of this regulatory mechanism to a subset of Gram-negative bacteria.


  • Organizational Affiliation

    Laboratoire de Biologie et Génomique Structurales, IGBMC, BP163, 67404 Illkirch Cedex, France.


Macromolecules

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Threonyl-tRNA synthetase401Escherichia coliMutation(s): 0 
EC: 6.1.1.3
UniProt
Find proteins for P0A8M3 (Escherichia coli (strain K12))
Explore P0A8M3 
Go to UniProtKB:  P0A8M3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A8M3
Sequence Annotations
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  • Reference Sequence
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Entity ID: 1
MoleculeChains LengthOrganismImage
Threonyl-tRNA synthetase mRNA37N/A
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
TSB
Query on TSB

Download Ideal Coordinates CCD File 
BA [auth F]
DA [auth G]
FA [auth H]
R [auth A]
T [auth B]
BA [auth F],
DA [auth G],
FA [auth H],
R [auth A],
T [auth B],
V [auth C],
X [auth D],
Z [auth E]
5'-O-(N-(L-THREONYL)-SULFAMOYL)ADENOSINE
C14 H21 N7 O8 S
UPVAPSGKXAAHBG-CKTDUXNWSA-N
ZN
Query on ZN

Download Ideal Coordinates CCD File 
AA [auth F]
CA [auth G]
EA [auth H]
Q [auth A]
S [auth B]
AA [auth F],
CA [auth G],
EA [auth H],
Q [auth A],
S [auth B],
U [auth C],
W [auth D],
Y [auth E]
ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.287 
  • R-Value Work: 0.251 
  • R-Value Observed: 0.251 
  • Space Group: P 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 188.45α = 90
b = 101.74β = 114.4
c = 199.34γ = 90
Software Package:
Software NamePurpose
AMoREphasing
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2002-04-26
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-16
    Changes: Advisory, Data collection, Database references, Derived calculations, Refinement description