› 5vrg

X-ray diffraction
2.52Å resolution

Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase

Released:
DOI: 10.2210/pdb5vrg/pdb
PDB entry 5vrg coloured by chain, front view.
PDB entry 5vrg coloured by chain, side view.
PDB entry 5vrg coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase.
Noland CL, Kattke MD, Diao J, Gloor SL, Pantua H, Reichelt M, Katakam AK, Yan D, Kang J, Zilberleyb I, Xu M, Kapadia SB, Murray JM
Proc Natl Acad Sci U S A 114 E6044-E6053 (2017)
PMID: 28698362

Function and Biology Details

Reaction catalysed: 
A phosphoglycerolipid + an [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine = a 1-lyso-phosphoglycerolipid + a [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150121 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipoprotein N-acyltransferase Chain: A
Molecule details ›
Chain: A
Length: 522 amino acids
Theoretical weight: 58.2 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P23930 (Residues: 2-512; Coverage: 100%)
Gene names: JW0654, b0657, cutE, lnt
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand OLC 1 x OLC
Ligand LNK 1 x LNK
Ligand PLM 5 x PLM
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 87.764Å b: 158.026Å c: 44.763Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.212 0.271
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.
Bahr et al. (2021)
3 more

2 mentions without citation

Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase.
Noland et al. (2017)
1 more