2FTN

E. coli thymidylate synthase Y94F mutant

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.204 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.183 

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This is version 1.3 of the entry. See complete history. 


Literature

Structure of the Y94F mutant of Escherichia coli thymidylate synthase.

Roberts, S.A., Hyatt, D.C., Honts, J.E., Changchien, L., Maley, G.F., Maley, F., Montfort, W.R.

(2006) Acta Crystallogr Sect F Struct Biol Cryst Commun 62: 840-843

  • DOI: https://doi.org/10.1107/S1744309106029691
  • Primary Citation of Related Structures:  
    2FTN, 2FTO

  • PubMed Abstract: 

    Tyr94 of Escherichia coli thymidylate synthase is thought to be involved, either directly or by activation of a water molecule, in the abstraction of a proton from C5 of the 2'-deoxyuridine 5'-monophosphate (dUMP) substrate. Mutation of Tyr94 leads to a 400-fold loss in catalytic activity. The structure of the Y94F mutant has been determined in the native state and as a ternary complex with thymidine 5'-monophosphate (dTMP) and 10-propargyl 5,8-dideazafolate (PDDF). There are no structural changes ascribable to the mutation other than loss of a water molecule hydrogen bonded to the tyrosine OH, which is consistent with a catalytic role for the phenolic OH.

    • Organizational Affiliation: 

    Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, AZ 85721, USA.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Thymidylate synthase264Escherichia coliMutation(s): 2 
Gene Names: thyA
EC: 2.1.1.45
UniProt
Find proteins for P0A884 (Escherichia coli (strain K12))
Explore P0A884 
Go to UniProtKB:  P0A884
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A884
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.204 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.183 
  • Space Group: I 21 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 131.171α = 90
b = 131.171β = 90
c = 131.171γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
d*TREKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-05-02
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Derived calculations, Refinement description, Version format compliance
  • Version 1.3: 2021-10-20
    Changes: Database references, Derived calculations