1mm5

Solution NMR

Solution NMR structure of the outer membrane enzyme PagP in OG micelles

Released:
Source organism: Escherichia coli
Primary publication:
Solution structure and dynamics of the outer membrane enzyme PagP by NMR.
Proc. Natl. Acad. Sci. U.S.A. 99 13560-5 (2002)
PMID: 12357033

Function and Biology Details

Reaction catalysed:
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A = 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipid A palmitoyltransferase PagP Chain: A
Molecule details ›
Chain: A
Length: 170 amino acids
Theoretical weight: 20.2 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P37001 (Residues: 26-186; Coverage: 100%)
Gene names: JW0617, b0622, crcA, pagP, ybeG
Sequence domains: Antimicrobial peptide resistance and lipid A acylation protein PagP
Structure domains: Porin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)