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6YTC

Solution NMR structure of the isolated NTE domain of BT1762-63 levan transporter

Summary for 6YTC
Entry DOI10.2210/pdb6ytc/pdb
NMR InformationBMRB: 34514
DescriptorTonB-dependent receptor (1 entity in total)
Functional Keywordsglycan import, transporter, n-terminal domain, ig-like fold, protein transport
Biological sourceBacteroides thetaiotaomicron
Total number of polymer chains1
Total formula weight9947.12
Authors
Rath, P.,Mazur, A.,Hiller, S. (deposition date: 2020-04-24, release date: 2020-07-08, Last modification date: 2024-06-19)
Primary citationGray, D.A.,White, J.B.R.,Oluwole, A.O.,Rath, P.,Glenwright, A.J.,Mazur, A.,Zahn, M.,Basle, A.,Morland, C.,Evans, S.L.,Cartmell, A.,Robinson, C.V.,Hiller, S.,Ranson, N.A.,Bolam, D.N.,van den Berg, B.
Insights into SusCD-mediated glycan import by a prominent gut symbiont.
Nat Commun, 12:44-44, 2021
Cited by
PubMed Abstract: 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.
PubMed: 33398001
DOI: 10.1038/s41467-020-20285-y
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

数据于2024-10-30公开中

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