› 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 5nv8 coloured by chain and viewed from the front.
PDB 5nv8 coloured by chain and viewed from the side.
PDB 5nv8 coloured by chain and viewed from the top.
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
OpenAccess logo 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)
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

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Citations

1 review citation

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