Ontology highlight
ABSTRACT:
SUBMITTER: Hwang PM
PROVIDER: S-EPMC129713 | biostudies-literature | 2002 Oct
REPOSITORIES: biostudies-literature
Hwang Peter M PM Choy Wing-Yiu WY Lo Eileen I EI Chen Lu L Forman-Kay Julie D JD Raetz Christian R H CR Privé Gilbert G GG Bishop Russell E RE Kay Lewis E LE
Proceedings of the National Academy of Sciences of the United States of America 20020930 21
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 of an eight-stranded anti-parallel beta-barrel prece ...[more]