Journal article
Solution structure and dynamics of the outer membrane enzyme PagP by NMR
Abstract
The bacterial outer membrane enzyme PagP transfers a palmitate chain from a phospholipid to lipid A. In a number of pathogenic Gram-negative bacteria, PagP confers resistance to certain cationic antimicrobial peptides produced during the host innate immune response. The global fold of Escherichia coli PagP was determined in both dodecylphosphocholine and n-octyl-beta-d-glucoside detergent micelles using solution NMR spectroscopy. PagP consists …
Authors
Hwang PM; Choy W-Y; Lo EI; Chen L; Forman-Kay JD; Raetz CRH; Privé GG; Bishop RE; Kay LE
Journal
Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, No. 21, pp. 13560–13565
Publisher
Proceedings of the National Academy of Sciences
Publication Date
October 15, 2002
DOI
10.1073/pnas.212344499
ISSN
0027-8424
Fields of Research (FoR)
Medical Subject Headings (MeSH)
AcyltransferasesAmino Acid SequenceBacterial Outer Membrane ProteinsEscherichia coliEscherichia coli ProteinsMicellesModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein FoldingProtein Structure, SecondarySequence Homology, Amino AcidSolutionsThermodynamics