› 1fmt

X-ray diffraction
2Å resolution

METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1fmt/pdb
PDB entry 1fmt coloured by chain, front view.
PDB entry 1fmt coloured by chain, side view.
PDB entry 1fmt coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase.
Schmitt E, Blanquet S, Mechulam Y
EMBO J 15 4749-58 (1996)
PMID: 8887566

Function and Biology Details

Reaction catalysed: 
10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150093 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionyl-tRNA formyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 314 amino acids
Theoretical weight: 34.07 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P23882 (Residues: 2-315; Coverage: 100%)
Gene names: JW3249, b3288, fmt, yhdD
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P3221
Unit cell:
a: 151.04Å b: 151.04Å c: 81.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.214 0.214 0.256
Expression system: Escherichia coli

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Citations

9 review citations

Aminoacyl-tRNA synthesis.
Ibba et al. (2000)
8 more

8 mentions without citation

A nonredundant structure dataset for benchmarking protein-RNA computational docking.
Huang et al. (2013)
7 more