2FMT

METHIONYL-TRNAFMET FORMYLTRANSFERASE COMPLEXED WITH FORMYL-METHIONYL-TRNAFMET


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.292 
  • R-Value Work: 0.247 
  • R-Value Observed: 0.247 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet.

Schmitt, E.Panvert, M.Blanquet, S.Mechulam, Y.

(1998) EMBO J 17: 6819-6826

  • DOI: https://doi.org/10.1093/emboj/17.23.6819
  • Primary Citation of Related Structures:  
    2FMT

  • PubMed Abstract: 

    The crystal structure of Escherichia coli methionyl-tRNAfMet transformylase complexed with formyl-methionyl-tRNAfMet was solved at 2.8 A resolution. The formylation reaction catalyzed by this enzyme irreversibly commits methionyl-tRNAfMet to initiation of translation in eubacteria. In the three-dimensional model, the methionyl-tRNAfMet formyltransferase fills in the inside of the L-shaped tRNA molecule on the D-stem side. The anticodon stem and loop are away from the protein. An enzyme loop is wedged in the major groove of the acceptor helix. As a result, the C1-A72 mismatch characteristic of the initiator tRNA is split and the 3' arm bends inside the active centre. This recognition mechanism is markedly distinct from that of elongation factor Tu, which binds the acceptor arm of aminoacylated elongator tRNAs on the T-stem side.


  • Organizational Affiliation

    Laboratoire de Biochimie, Unité Mixte de Recherche No. 7654 du Centre National de la Recherche Scientifique, Ecole Polytechnique, F-91128 Palaiseau cedex, France.


Macromolecules

Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
METHIONYL-TRNA FMET FORMYLTRANSFERASEC [auth A],
D [auth B]
314Escherichia coliMutation(s): 0 
Gene Names: FMT
EC: 2.1.2.9
UniProt
Find proteins for P23882 (Escherichia coli (strain K12))
Explore P23882 
Go to UniProtKB:  P23882
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP23882
Sequence Annotations
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  • Reference Sequence
Find similar nucleic acids by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains LengthOrganismImage
FORMYL-METHIONYL-TRNAFMET2A [auth C],
B [auth D]
77synthetic construct
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.292 
  • R-Value Work: 0.247 
  • R-Value Observed: 0.247 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 201.71α = 90
b = 68.06β = 90
c = 86.35γ = 90
Software Package:
Software NamePurpose
SHARPphasing
CNSrefinement
MOSFLMdata reduction
CCP4data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-07-29
    Type: Initial release
  • Version 1.1: 2008-05-22
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2020-02-19
    Changes: Derived calculations, Source and taxonomy
  • Version 1.4: 2023-08-02
    Changes: Database references, Derived calculations, Refinement description