› 5nv8

X-ray diffraction
2.29Å resolution

Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P

Released:
DOI: 10.2210/pdb5nv8/pdb
PDB entry 5nv8 coloured by chain, front view.
PDB entry 5nv8 coloured by chain, side view.
PDB entry 5nv8 coloured by chain, top view.
Source organism: Pseudomonas putida KT2440
Primary publication:
Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P.
Krafczyk R, Macošek J, Jagtap PKA, Gast D, Wunder S, Mitra P, Jha AK, Rohr J, Hoffmann-Röder A, Jung K, Hennig J, Lassak J
mBio 8 (2017)
PMID: 28951478

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183493 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-arginine rhamnosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 390 amino acids
Theoretical weight: 43.68 KDa
Source organism: Pseudomonas putida KT2440
Expression system: Escherichia coli
UniProt:
  • Canonical: Q88LS1 (Residues: 2-377; Coverage: 100%)
Gene names: PP_1857, earP
Sequence domains: Elongation-Factor P (EF-P) rhamnosyltransferase EarP

Ligands and Environments

1 bound ligand:
Ligand TRH 1 x TRH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: I4
Unit cell:
a: 131.68Å b: 131.68Å c: 46.24Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.292 0.289 0.339
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Bacteria-Catalyzed Arginine Glycosylation in Pathogens and Host.
Pan et al. (2020)
6 other articles

2 mentions without citation

TmAlphaFold database: membrane localization and evaluation of AlphaFold2 predicted alpha-helical transmembrane protein structures.
Dobson et al. (2023)
1 more