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TitleStructural basis of lipopolysaccharide maturation by the O-antigen ligase.
Journal, issue, pagesNature, Vol. 604, Issue 7905, Page 371-376, Year 2022
Publish dateApr 6, 2022
AuthorsKhuram 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 /
PubMed AbstractThe 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.
External linksNature / PubMed:35388216 / PubMed Central
MethodsEM (single particle)
Resolution3.23 - 3.46 Å
Structure data

26054

7tpg

EMDB-26054, PDB-7tpg:
Single-Particle Cryo-EM Structure of the WaaL O-antigen ligase in its ligand bound state
Method: EM (single particle) / Resolution: 3.23 Å

26057

7tpj

EMDB-26057, PDB-7tpj:
Single-Particle Cryo-EM Structure of the WaaL O-antigen ligase in its apo state
Method: EM (single particle) / Resolution: 3.46 Å

Chemicals

ChemComp-GPP:
GERANYL DIPHOSPHATE / Geranyl pyrophosphate

Source
  • cupriavidus metallidurans (bacteria)
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Lipopolysaccharide / single-particle cryo-electron microscopy / molecular dynamics simulations / structural biology / undecaprenyl pyrophosphate / WaaL Ligase / lipid A / O-antigen / membrane proteins / transglycosylation / glycosyltransferase

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