› 2z3m

X-ray diffraction
2.7Å resolution

complex structure of LF-transferase and dAF

Released:
DOI: 10.2210/pdb2z3m/pdb
PDB entry 2z3m coloured by chain, front view.
PDB entry 2z3m coloured by chain, side view.
PDB entry 2z3m coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase.
Watanabe K, Toh Y, Suto K, Shimizu Y, Oka N, Wada T, Tomita K
Nature 449 867-71 (2007)
PMID: 17891155

Function and Biology Details

Reaction catalysed: 
L-leucyl-tRNA(Leu) + N-terminal L-arginyl-[protein] = tRNA(Leu) + N-terminal L-leucyl-L-arginyl-[protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141720 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucyl/phenylalanyl-tRNA--protein transferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 233 amino acids
Theoretical weight: 26.52 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A8P1 (Residues: 2-234; Coverage: 100%)
Gene names: JW0868, aat, b0885, ycaA
Sequence domains: Leucyl/phenylalanyl-tRNA protein transferase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand 3D1 2 x 3D1
Ligand PHE 2 x PHE
Ligand TAR 2 x TAR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21212
Unit cell:
a: 116.681Å b: 127.682Å c: 38.354Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.261
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

The N-end rule pathway and regulation by proteolysis.
Varshavsky A. (2011)
16 more