RT Journal Article
SR Electronic
T1 Structural basis for lipid transport by the MLA complex
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.05.30.125013
DO 10.1101/2020.05.30.125013
A1 Daniel Mann
A1 Junping Fan
A1 Daniel P. Farrell
A1 Kamolrat Somboon
A1 Andrew Muenks
A1 Svetomir B. Tzokov
A1 Syma Khalid
A1 Frank Dimaio
A1 Samuel I. Miller
A1 Julien R. C. Bergeron
YR 2020
UL http://biorxiv.org/content/early/2020/05/31/2020.05.30.125013.abstract
AB The maintenance of lipid asymmetry (MLA) system is involved in lipid transport from/to the outer membrane in gram-negative bacteria, and contributes to broad-range antibiotic resistance. Here, we report the cryo-EM structure of the A. baumannii MlaBDEF core complex, in the apo, ADP- and AppNHp-bound states. This reveals multiple lipid binding sites, and suggests a mechanism for their transport.Competing Interest StatementThe authors have declared no competing interest.