Solution Structure and Dynamics of the Outer Membrane Enzyme PagP by NMR

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 co...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2002-10, Vol.99 (21), p.13560-13565
Hauptverfasser:	Hwang, Peter M., Choy, Wing-Yiu, Lo, Eileen I., Chen, Lu, Forman-Kay, Julie D., Christian R. H. Raetz, Privé, Gilbert G., Bishop, Russell E., Kay, Lewis E.
Format:	Artikel
Sprache:	eng
Schlagworte:	Active sites Acyltransferases - chemistry Acyltransferases - genetics Amino Acid Sequence Bacteria Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - genetics Biochemistry Biological Sciences Detergents Enzymes Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Infections Lipids Membranes Micelles Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Nuclear Magnetic Resonance, Biomolecular Palmitates Phospholipids Protein Conformation Protein Folding Protein Structure, Secondary Sequence Homology, Amino Acid Sodium Solutions Thermodynamics
Online-Zugang:	Volltext
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