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PMID: 22819666 Published · ppublish English Journal Article Review

Glycan recognition by the Bacteroidetes Sus-like systems.

Current opinion in structural biology ·Vol. 22 ·No. 5 ·2012-10-00 ·Pages 563-9

Bolam DN, Koropatkin NM

Abstract

The human gut Bacteroidetes employ multiple cell-envelope associated protein complexes, termed Sus-like systems, to capture and degrade glycans. Recently the structures of key glycan-binding Sus proteins, the surface located SusD proteins and the periplasmic sensor domains of the membrane spanning hybrid two-component systems (HTCS) controlling Sus expression, have been solved, providing insight into glycan acquisition and sensing in these symbionts. The α-helical SusD proteins bind glycans at the cell surface, and likely facilitate the shuttling of oligosaccharides to an associated TonB-dependent porin. The HTCS sensor domains adopt two distinct folds and the structures of these sensors with glycan suggest that signal transduction across the cytoplasmic membrane is different from classical two component systems.

MeSH Terms
Bacterial Proteins/chemistry,metabolism Bacteroidetes Extracellular Space/metabolism Humans Polysaccharides/metabolism Protein Binding
Chemicals
Bacterial Proteins Polysaccharides
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bolam David N
Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, United Kingdom.
Koropatkin Nicole M
Article Info
Journal
Current opinion in structural biology
Abbr.
Curr Opin Struct Biol
ISSN
1879-033X
Published
2012-10-00
Epub
2012-00-19
Pages
563-9
Language
English
Region
England
NLM ID
9107784
Subset
IM
Grants
Biotechnology and Biological Sciences Research Council · BB/F014163/1 · United Kingdom
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