Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 34272394Publication DOI: 10.1038/s41467-021-24652-1Journal NLM ID: 101528555Publisher: London: Nature Publishing Group
Correspondence: cwhitfie
uoguelph.ca; naismith
strubi.ox.ac.uk
Institutions: Rosalind Franklin Institute, Harwell Campus, Harwell, UK, Division of Structural Biology, The University of Oxford, Oxford, UK, The Research Complex at Harwell, Harwell Campus, Harwell, UK, Department of Molecular and Cellular Biology, The University of Guelph, Guelph, ON, Canada, Physical and Theoretical Chemistry Laboratory, Department of Chemistry, South Parks Road, The University of Oxford, Oxford, UK, The Kavli Institute for Nanoscience Discovery, Oxford, UK, Electron Bio-Imaging Centre, Diamond Light Source, Harwell Science and Innovation Campus, Harwell, UK
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.
virulence, assembly, capsule, bacterial extracellular polysaccharides
Structure type: polymer chemical repeating unit
Location inside paper: Fig. 1a
Compound class: CPS
Contained glycoepitopes: IEDB_115136,IEDB_130701,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_144983,IEDB_151528,IEDB_152206,IEDB_190606,IEDB_423153,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_36,SB_44,SB_67,SB_7,SB_72,SB_88
Methods: gel filtration, SDS-PAGE, Western blotting, genetic methods, cloning, expression, cryo-EM analysis, phosphoproteomics analysis, phosphopeptide analysis
3D data: 3D data
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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