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Structure paper

TitleInsights into SusCD-mediated glycan import by a prominent gut symbiont.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 44, Year 2021
Publish dateJan 4, 2021
AuthorsDeclan A Gray / Joshua B R White / Abraham O Oluwole / Parthasarathi Rath / Amy J Glenwright / Adam Mazur / Michael Zahn / Arnaud Baslé / Carl Morland / Sasha L Evans / Alan Cartmell / Carol V Robinson / Sebastian Hiller / Neil A Ranson / David N Bolam / Bert van den Berg /
PubMed AbstractIn 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 ...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.
External linksNat Commun / PubMed:33398001 / PubMed Central
MethodsEM (single particle) / NMR (solution) / X-ray diffraction
Resolution2.62 - 4.7 Å
Structure data

11273

6zlt

EMDB-11273, PDB-6zlt:
Open-open state of the Bt1762-Bt1763 levan transport system
Method: EM (single particle) / Resolution: 3.9 Å

11274

6zlu

EMDB-11274, PDB-6zlu:
Closed-closed state of the Bt1762-Bt1763 levan transport system
Method: EM (single particle) / Resolution: 4.2 Å

11277

6zm1

EMDB-11277, PDB-6zm1:
Open-closed state of the Bt1762-Bt1763 levan transport system
Method: EM (single particle) / Resolution: 4.7 Å

PDB-6ytc:
Solution NMR structure of the isolated NTE domain of BT1762-63 levan transporter
Method: SOLUTION NMR

PDB-6z8i:
Fructo-oligosaccharide transporter BT 1762-63
Method: X-RAY DIFFRACTION / Resolution: 2.62 Å

PDB-6z9a:
Fructo-oligosaccharide transporter BT 1762-63
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-6zaz:
Fructo-oligosaccharide transporter BT 1762-63
Method: X-RAY DIFFRACTION / Resolution: 2.69 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

ChemComp-C8E:
(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE / C8E, detergent*YM

Source
  • bacteroides thetaiotaomicron (strain atcc 29148 / dsm 2079 / nctc 10582 / e50 / vpi-5482) (bacteria)
  • bacteroides thetaiotaomicron (bacteria)
KeywordsPROTEIN TRANSPORT / Glycan import / Transporter / N-terminal Domain / Ig-like fold / MEMBRANE PROTEIN / Outer membrane protein TonB-dependent transporter SusC SusD Levan Bacteroides thetaiotaomicron / SusCD / Levan / TonB-dependent

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