6RBG

full-length bacterial polysaccharide co-polymerase

Summary for 6RBG

• Entry DOI: 10.2210/pdb6rbg/pdb
• EMDB information: 4791 4798
• Descriptor: Chain length determinant protein (1 entity in total)
• Functional Keywords: membrane protein, enzyme, polysaccharide, co-polymerase
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 8
• Total formula weight: 306964.97

Authors

Wiseman, B.,Nitharwal, R.G.,Hogbom, M. (deposition date: 2019-04-10, release date: 2020-11-18, Last modification date: 2024-05-22)

Primary citation

Wiseman, B.,Nitharwal, R.G.,Widmalm, G.,Hogbom, M.
Structure of a full-length bacterial polysaccharide co-polymerase.
Nat Commun, 12:369-369, 2021

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 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.

PubMed: 33446644
DOI: 10.1038/s41467-020-20579-1

Experimental method

ELECTRON MICROSCOPY (3 Å)