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Structure and mechanism of an active lipid-linked oligosaccharide flippase

Perez, Camilo and Gerber, Sabina and Boilevin, Jérémy and Bucher, Monika and Darbre, Tamis and Aebi, Markus and Reymond, Jean-Louis and Locher, Kaspar P.. (2015) Structure and mechanism of an active lipid-linked oligosaccharide flippase. Nature, 524 (7566). pp. 433-438.

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Official URL: http://edoc.unibas.ch/56040/

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Abstract

The flipping of membrane-embedded lipids containing large, polar head groups is slow and energetically unfavourable, and is therefore catalysed by flippases, the mechanisms of which are unknown. A prominent example of a flipping reaction is the translocation of lipid-linked oligosaccharides that serve as donors in N-linked protein glycosylation. In Campylobacter jejuni, this process is catalysed by the ABC transporter PglK. Here we present a mechanism of PglK-catalysed lipid-linked oligosaccharide flipping based on crystal structures in distinct states, a newly devised in vitro flipping assay, and in vivo studies. PglK can adopt inward- and outward-facing conformations in vitro, but only outward-facing states are required for flipping. While the pyrophosphate-oligosaccharide head group of lipid-linked oligosaccharides enters the translocation cavity and interacts with positively charged side chains, the lipidic polyprenyl tail binds and activates the transporter but remains exposed to the lipid bilayer during the reaction. The proposed mechanism is distinct from the classical alternating-access model applied to other transporters.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics
UniBasel Contributors:Perez, Camilo
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Nature Publishing Group
ISSN:0028-0836
e-ISSN:1476-4687
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:26 Oct 2017 15:51
Deposited On:26 Oct 2017 15:51

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