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Structure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate binding

Anandan, Anandhi; Evans, Genevieve L.; Condic-Jurkic, Karmen; O'Mara, Megan; John, Constance M.; Phillips, Nancy J.; Jarvis, Gary A.; Wills, Siobhan S.; Stubbs, Keith A.; Moraes, Isabel; Kahler, Charlene M.; Vrielink, Alice

Description

Multidrug-resistant (MDR) gram-negative bacteria have increased the prevalence of fatal sepsis in modern times. Colistin is a cationic antimicrobial peptide (CAMP) antibiotic that permeabilizes the bacterial outer membrane (OM) and has been used to treat these infections. The OM outer leaflet is comprised of endotoxin containing lipid A, which can be modified to increase resistance to CAMPs and prevent clearance by the innate immune response. One type of lipid A modification involves the...[Show more]

CollectionsANU Research Publications
Date published: 2017-02-13
Type: Journal article
URI: http://hdl.handle.net/1885/234613
Source: PNAS - Proceedings of the National Academy of Sciences of the United States of America
DOI: 10.1073/pnas.1612927114

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