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Published on: June 28, 2013
Structure of a full-length bacterial polysaccharide co-polymerase
Benjamin Wiseman1, Ram Gopal Nitharwal2,3, Göran Widmalm4
1Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden. bwise@dbb.su.se.
The bacterial WzzB protein structure reveals its octameric, jellyfish-like architecture. This finding clarifies the Wzy-dependent pathway essential for bacterial cell envelope formation and antibiotic resistance.
Area of Science:
- Structural Biology
- Microbiology
- Biochemistry
Background:
- Lipopolysaccharides are crucial bacterial cell envelope components, acting as protective barriers.
- The Wzy-dependent pathway is a widespread mechanism for polysaccharide biosynthesis in bacteria.
Purpose of the Study:
- To determine the 3.0 Å structure of WzzB, the co-polymerase component of the Wzy-dependent pathway.
- To elucidate the architecture of WzzB and its transmembrane domain.
Main Methods:
- Single-particle cryo-electron microscopy was employed to solve the structure of WzzB from E. coli.
Main Results:
- The study presents the octameric structure of WzzB, resembling a box jellyfish.
- A large, bell-shaped periplasmic domain and a 2-helix transmembrane domain encircling a transmembrane chamber were identified.
- The structure reveals key residues within the transmembrane domain relevant to Wzz-family proteins and the Wzy-dependent pathway.
Conclusions:
- The determined structure provides insights into the Wzy-dependent pathway's mechanism.
- This work explains previous biochemical and mutational studies on WzzB.
- The findings lay the groundwork for future research into bacterial cell envelope biosynthesis and antibiotic resistance.
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