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The molecular basis of regulation of bacterial capsule assembly by Wzc

DOI: 10.1038/s41467-021-24652-1 DOI Help

Authors: Yun Yang (Rosalind Franklin Institute; The University of Oxford; The Research Complex at Harwell) , Jiwei Liu (Rosalind Franklin Institute; The University of Oxford) , Bradley R. Clarke (The University of Guelph) , Laura Seidel (The University of Guelph) , Jani R. Bolla (The University of Oxford; The Kavli Institute for Nanoscience Discovery) , Philip N. Ward (Rosalind Franklin Institute; The University of Oxford; The Research Complex at Harwell) , Peijun Zhang (The University of Oxford; Diamond Light Source) , Carol V. Robinson (The University of Oxford; The Kavli Institute for Nanoscience Discovery) , Chris Whitfield (The University of Guelph) , James Naismith (Rosalind Franklin Institute; The University of Oxford; The Research Complex at Harwell)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 12

State: Published (Approved)
Published: July 2021
Diamond Proposal Number(s): 20223

Open Access Open Access

Abstract: Bacterial extracellular polysaccharides (EPSs) play critical roles in virulence. Many bacteria assemble EPSs via a multi-protein “Wzx-Wzy” system, involving glycan polymerization at the outer face of the cytoplasmic/inner membrane. Gram-negative species couple polymerization with translocation across the periplasm and outer membrane and the master regulator of the system is the tyrosine autokinase, Wzc. This near atomic cryo-EM structure of dephosphorylated Wzc from E. coli shows an octameric assembly with a large central cavity formed by transmembrane helices. The tyrosine autokinase domain forms the cytoplasm region, while the periplasmic region contains small folded motifs and helical bundles. The helical bundles are essential for function, most likely through interaction with the outer membrane translocon, Wza. Autophosphorylation of the tyrosine-rich C-terminus of Wzc results in disassembly of the octamer into multiply phosphorylated monomers. We propose that the cycling between phosphorylated monomer and dephosphorylated octamer regulates glycan polymerization and translocation.

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: Krios I-Titan Krios I at Diamond

Documents:
s41467-021-24652-1.pdf

Discipline Tags:

Pathogens Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Microscopy Electron Microscopy (EM) Cryo Electron Microscopy (Cryo EM)