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Solution NMR

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

Released:
DOI: 10.2210/pdb1mm4/pdb
PDB entry 1mm4 coloured by chain, ensemble of 20 models, front view.
PDB entry 1mm4 coloured by chain, ensemble of 20 models, side view.
PDB entry 1mm4 coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
Solution structure and dynamics of the outer membrane enzyme PagP by NMR.
Hwang PM, Choy WY, Lo EI, Chen L, Forman-Kay JD, Raetz CR, Privé GG, Bishop RE, Kay LE
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
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153282 (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)

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Citations

49 review citations

Molecular basis of bacterial outer membrane permeability revisited.
Nikaido H. (2003)
48 more

10 mentions without citation

The structural biology of β-barrel membrane proteins: a summary of recent reports.
Fairman et al. (2011)
9 more