National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM132120
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI150098
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI138576
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI129940
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM117372
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM116799
United States
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)
DK104309
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI100852
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI146284
United States
Wellcome Trust
208361/Z/17/Z
United Kingdom
Medical Research Council (MRC, United Kingdom)
MR/S009213/1
United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/P01948X/1
United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/R002517/1
United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/S003339/1
United Kingdom
Engineering and Physical Sciences Research Council
EP/R029407/1
United Kingdom
Engineering and Physical Sciences Research Council
EP/P020232/1
United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/M01116X/1
United Kingdom
Medical Research Council (MRC, United Kingdom)
MR/N002679/1
United Kingdom
Citation
Journal: Nature / Year: 2022 Title: Structural basis of lipopolysaccharide maturation by the O-antigen ligase. Authors: Khuram U Ashraf / Rie Nygaard / Owen N Vickery / Satchal K Erramilli / Carmen M Herrera / Thomas H McConville / Vasileios I Petrou / Sabrina I Giacometti / Meagan Belcher Dufrisne / Kamil ...Authors: Khuram U Ashraf / Rie Nygaard / Owen N Vickery / Satchal K Erramilli / Carmen M Herrera / Thomas H McConville / Vasileios I Petrou / Sabrina I Giacometti / Meagan Belcher Dufrisne / Kamil Nosol / Allen P Zinkle / Chris L B Graham / Michael Loukeris / Brian Kloss / Karolina Skorupinska-Tudek / Ewa Swiezewska / David I Roper / Oliver B Clarke / Anne-Catrin Uhlemann / Anthony A Kossiakoff / M Stephen Trent / Phillip J Stansfeld / Filippo Mancia / Abstract: The outer membrane of Gram-negative bacteria has an external leaflet that is largely composed of lipopolysaccharide, which provides a selective permeation barrier, particularly against antimicrobials. ...The outer membrane of Gram-negative bacteria has an external leaflet that is largely composed of lipopolysaccharide, which provides a selective permeation barrier, particularly against antimicrobials. The final and crucial step in the biosynthesis of lipopolysaccharide is the addition of a species-dependent O-antigen to the lipid A core oligosaccharide, which is catalysed by the O-antigen ligase WaaL. Here we present structures of WaaL from Cupriavidus metallidurans, both in the apo state and in complex with its lipid carrier undecaprenyl pyrophosphate, determined by single-particle cryo-electron microscopy. The structures reveal that WaaL comprises 12 transmembrane helices and a predominantly α-helical periplasmic region, which we show contains many of the conserved residues that are required for catalysis. We observe a conserved fold within the GT-C family of glycosyltransferases and hypothesize that they have a common mechanism for shuttling the undecaprenyl-based carrier to and from the active site. The structures, combined with genetic, biochemical, bioinformatics and molecular dynamics simulation experiments, offer molecular details on how the ligands come in apposition, and allows us to propose a mechanistic model for catalysis. Together, our work provides a structural basis for lipopolysaccharide maturation in a member of the GT-C superfamily of glycosyltransferases.
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