› 2cxa

X-ray diffraction
1.6Å resolution

Crystal structure of Leucyl/phenylalanyl-tRNA protein transferase from Escherichia coli

Released:
DOI: 10.2210/pdb2cxa/pdb
PDB entry 2cxa coloured by chain, front view.
PDB entry 2cxa coloured by chain, side view.
PDB entry 2cxa coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The crystal structure of leucyl/phenylalanyl-tRNA-protein transferase from Escherichia coli.
Dong X, Kato-Murayama M, Muramatsu T, Mori H, Shirouzu M, Bessho Y, Yokoyama S
Protein Sci. 16 528-34 (2007)
PMID: 17242373

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141719 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucyl/phenylalanyl-tRNA--protein transferase Chain: A
Molecule details ›
Chain: A
Length: 256 amino acids
Theoretical weight: 29.55 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A8P1 (Residues: 1-234; Coverage: 100%)
Gene names: JW0868, aat, b0885, ycaA
Sequence domains: Leucyl/phenylalanyl-tRNA protein transferase
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 9 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2
Unit cell:
a: 68.277Å b: 44.784Å c: 76.376Å
α: 90° β: 108.36° γ: 90°
R-values:
R R work R free
0.187 0.187 0.217
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

4 mentions without citation

Interplay of hydrogen bonds and n→π* interactions in proteins.
Bartlett et al. (2013)
3 more