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Structural Studies on the Lipid Flippase MurJ

dc.contributor.advisor Lee, Seok-Yong
dc.contributor.author Kuk, Alvin Chun Yin
dc.date.accessioned 2019-04-02T16:27:37Z
dc.date.issued 2018
dc.identifier.uri https://hdl.handle.net/10161/18266
dc.description Dissertation
dc.description.abstract <p>The biosynthesis of many important polysaccharides (including peptidoglycan, lipopolysaccharide, and N-linked glycans) necessitates membrane transport of oligosaccharide precursors from their cytoplasmic site of synthesis to their site of assembly outside the cytoplasm. To address this problem, cells utilize transporters such as those of the multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) superfamily to flip lipid-linked oligosaccharides across the cytoplasmic membrane. The MOP superfamily member MurJ has been shown to be the flippase that transports the lipid-linked peptidoglycan precursor lipid II, but the lack of structural information has limited our mechanistic understanding of the MurJ transport cycle. We determined the first crystal structure of MurJ (MurJTA from Thermosipho africanus) to 2.0-Å resolution, which assumed an inward-facing conformation unlike all other outward-facing structures of MOP transporters. Our structural and mutagenesis studies provide insight into a putative model of lipid II binding and an alternating-access mechanism of transport.</p>
dc.subject Biochemistry
dc.subject Biophysics
dc.subject Molecular biology
dc.subject cell wall
dc.subject flippase
dc.subject membrane protein
dc.subject peptidoglycan
dc.subject transporter
dc.subject X-ray crystallography
dc.title Structural Studies on the Lipid Flippase MurJ
dc.type Dissertation
dc.department Biochemistry
duke.embargo.months 21
duke.embargo.release 2021-01-09T00:00:00Z


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