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-Structure paper
Title | Structure of a full-length bacterial polysaccharide co-polymerase. |
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Journal, issue, pages | Nat Commun, Vol. 12, Issue 1, Page 369, Year 2021 |
Publish date | Jan 14, 2021 |
Authors | Benjamin Wiseman / Ram Gopal Nitharwal / Göran Widmalm / Martin Högbom / |
PubMed Abstract | Lipopolysaccharides are important components of the bacterial cell envelope that among other things act as a protective barrier against the environment and toxic molecules such as antibiotics. One of ...Lipopolysaccharides are important components of the bacterial cell envelope that among other things act as a protective barrier against the environment and toxic molecules such as antibiotics. One of the most widely disseminated pathways of polysaccharide biosynthesis is the inner membrane bound Wzy-dependent pathway. Here we present the 3.0 Å structure of the co-polymerase component of this pathway, WzzB from E. coli solved by single-particle cryo-electron microscopy. The overall architecture is octameric and resembles a box jellyfish containing a large bell-shaped periplasmic domain with the 2-helix transmembrane domain from each protomer, positioned 32 Å apart, encircling a large empty transmembrane chamber. This structure also reveals the architecture of the transmembrane domain, including the location of key residues for the Wzz-family of proteins and the Wzy-dependent pathway present in many Gram-negative bacteria, explaining several of the previous biochemical and mutational studies and lays the foundation for future investigations. |
External links | Nat Commun / PubMed:33446644 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.0 - 7.2 Å |
Structure data | EMDB-11908: EMDB-11909: EMDB-4791: |
Source |
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Keywords | MEMBRANE PROTEIN / enzyme / polysaccharide / co-polymerase |