› 5n6h

X-ray diffraction
2.9Å resolution

Structure of the membrane integral lipoprotein N-acyltransferase Lnt from E. coli

Released:
DOI: 10.2210/pdb5n6h/pdb
PDB entry 5n6h coloured by chain, front view.
PDB entry 5n6h coloured by chain, side view.
PDB entry 5n6h coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis.
Wiktor M, Weichert D, Howe N, Huang CY, Olieric V, Boland C, Bailey J, Vogeley L, Stansfeld PJ, Buddelmeijer N, Wang M, Caffrey M
Nat Commun 8 15952 (2017)
PMID: 28675161

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 532 amino acids
Theoretical weight: 59.28 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P23930 (Residues: 1-512; Coverage: 100%)
Gene names: JW0654, b0657, cutE, lnt
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand OLC 18 x OLC
Ligand GOL 13 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 54.2Å b: 142.3Å c: 199.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.219 0.249
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structure and Mechanism of DHHC Protein Acyltransferases.
Stix et al. (2020)
2 more

7 mentions without citation

Bacterial Lipoprotein Posttranslational Modifications. New Insights and Opportunities for Antibiotic and Vaccine Development.
Smithers et al. (2021)
6 more