7NII

Wzc-K540M MgADP C1

Summary for 7NII

• Entry DOI: 10.2210/pdb7nii/pdb
• EMDB information: 12360
• Descriptor: Putative transmembrane protein Wzc, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• Functional Keywords: wzc, regulator, capsular polysaccharide synthesis and transport, gram-negative pathogens, carbohydrate
• Biological source: Escherichia coli
• Total number of polymer chains: 8
• Total formula weight: 648182.67

Authors

Naismith, J.H.,Liu, J.W.,Yang, Y. (deposition date: 2021-02-12, release date: 2021-08-25, Last modification date: 2024-07-10)

Primary citation

Yang, Y.,Liu, J.,Clarke, B.R.,Seidel, L.,Bolla, J.R.,Ward, P.N.,Zhang, P.,Robinson, C.V.,Whitfield, C.,Naismith, J.H.
The molecular basis of regulation of bacterial capsule assembly by Wzc.
Nat Commun, 12:4349-4349, 2021

PubMed 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.

PubMed: 34272394
DOI: 10.1038/s41467-021-24652-1

Experimental method

ELECTRON MICROSCOPY (2.88 Å)