@misc{gray_white_oluwole_rath_glenwright_mazur_zahn_basle_morland_evans_et al._2020, 
  title={Insights into glycan import by a prominent gut symbiont}, 
  DOI={10.1101/2020.06.11.146753}, 
  abstractNote={<jats:p>In Bacteroidetes, one of the dominant phyla of the mammalian gut, active uptake of large nutrients across the outer membrane is mediated by SusCD protein complexes via a pedal bin transport mechanism. However, many features of SusCD function in glycan uptake remain unclear, including ligand binding, the role of the SusD lid and the size limit for substrate transport. Here we characterise the β2,6 fructo-oligosaccharide (FOS) importing SusCD from Bacteroides thetaiotaomicron (Bt1762-Bt1763) to shed light on SusCD function. Co-crystal structures reveal residues involved in glycan recognition and suggest that the large binding cavity can accommodate several substrate molecules, each up to 2.5 kDa in size, a finding supported by native mass spectrometry and isothermal titration calorimetry. Mutational studies in vivo provide functional insights into the key structural features of the SusCD apparatus and cryo-EM of the intact dimeric SusCD complex reveals several distinct states of the transporter, directly visualising the dynamics of the pedal bin transport mechanism.</jats:p>}, 
  publisher={Cold Spring Harbor Laboratory}, 
  author={Gray, Declan and White, Joshua and Oluwole, Abraham and Rath, Parthasarathi and Glenwright, Amy and Mazur, Adam and Zahn, Michael and Basle, Arnaud and Morland, Carl and Evans, Sasha and et al.}, 
  year={2020}, 
  month={Jun}
  }