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TitleAlternating L4 loop architecture of the bacterial polysaccharide co-polymerase WzzE.
Journal, issue, pagesCommun Biol, Vol. 6, Issue 1, Page 802, Year 2023
Publish dateAug 2, 2023
AuthorsBenjamin Wiseman / Göran Widmalm / Martin Högbom /
PubMed AbstractLipopolysaccharides such as the enterobacterial common antigen are important components of the enterobacterial cell envelope that act as a protective barrier against the environment and are often ...Lipopolysaccharides such as the enterobacterial common antigen are important components of the enterobacterial cell envelope that act as a protective barrier against the environment and are often polymerized by the inner membrane bound Wzy-dependent pathway. By employing cryo-electron microscopy we show that WzzE, the co-polymerase component of this pathway that is responsible for the length modulation of the enterobacterial common antigen, is octameric with alternating up-down conformations of its L4 loops. The alternating up-down nature of these essential loops, located at the top of the periplasmic bell, are modulated by clashing helical faces between adjacent protomers that flank the L4 loops around the octameric periplasmic bell. This alternating arrangement and a highly negatively charged binding face create a dynamic environment in which the polysaccharide chain is extended, and suggest a ratchet-type mechanism for polysaccharide elongation.
External linksCommun Biol / PubMed:37532793 / PubMed Central
MethodsEM (single particle)
Resolution2.5 - 3.5 Å
Structure data

EMDB-16071, PDB-8bhw:
Full-length bacterial polysaccharide co-polymerase WzzE from E. coli. C4 symmetry
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-16072: Full-length bacterial polysaccharide co-polymerase WzzE from E. coli. C1 symmetry
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-16073: Full-length bacterial polysaccharide co-polymerase WzzE from E. coli. C8 symmetry
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-17387, PDB-8p3o:
Full-length bacterial polysaccharide co-polymerase WzzE mutant R267A from E. coli. C4 symmetry
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-17388: Full-length bacterial polysaccharide co-polymerase WzzE mutant R267A from E. coli. C1 symmetry
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-17389, PDB-8p3p:
Full-length bacterial polysaccharide co-polymerase WzzE mutant R267E from E. coli. C4 symmetry
Method: EM (single particle) / Resolution: 2.5 Å

EMDB-17390: Full-length bacterial polysaccharide co-polymerase WzzE mutant R267E from E. coli. C1 symmetry
Method: EM (single particle) / Resolution: 2.7 Å

Source
  • escherichia coli k-12 (bacteria)
KeywordsMEMBRANE PROTEIN / Complex / Lipopolysaccharide / bacterial polysaccharide co-polymerase

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