Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7ZNR

Inactive D62N mutant of BT1760 Endo-acting levanase from Bacteroides thetaiotaomicron VPI-5482

Summary for 7ZNR
Entry DOI10.2210/pdb7znr/pdb
DescriptorSucrose-6-phosphate hydrolase, beta-D-fructofuranose-(2-6)-beta-D-fructofuranose-(2-6)-beta-D-fructofuranose-(2-6)-beta-D-fructofuranose-(2-6)-beta-D-fructofuranose, beta-D-fructofuranose-(2-6)-beta-D-fructofuranose, ... (6 entities in total)
Functional Keywordslevan, fructan, endo levanase, gut microbiota, hydrolase
Biological sourceBacteroides thetaiotaomicron
Total number of polymer chains2
Total formula weight123083.52
Authors
Basle, A.,Bolam, D. (deposition date: 2022-04-21, release date: 2023-06-21, Last modification date: 2024-06-19)
Primary citationWhite, J.B.R.,Silale, A.,Feasey, M.,Heunis, T.,Zhu, Y.,Zheng, H.,Gajbhiye, A.,Firbank, S.,Basle, A.,Trost, M.,Bolam, D.N.,van den Berg, B.,Ranson, N.A.
Outer membrane utilisomes mediate glycan uptake in gut Bacteroidetes.
Nature, 618:583-589, 2023
Cited by
PubMed Abstract: Bacteroidetes are abundant members of the human microbiota, utilizing a myriad of diet- and host-derived glycans in the distal gut. Glycan uptake across the bacterial outer membrane of these bacteria is mediated by SusCD protein complexes, comprising a membrane-embedded barrel and a lipoprotein lid, which is thought to open and close to facilitate substrate binding and transport. However, surface-exposed glycan-binding proteins and glycoside hydrolases also play critical roles in the capture, processing and transport of large glycan chains. The interactions between these components in the outer membrane are poorly understood, despite being crucial for nutrient acquisition by our colonic microbiota. Here we show that for both the levan and dextran utilization systems of Bacteroides thetaiotaomicron, the additional outer membrane components assemble on the core SusCD transporter, forming stable glycan-utilizing machines that we term utilisomes. Single-particle cryogenic electron microscopy structures in the absence and presence of substrate reveal concerted conformational changes that demonstrate the mechanism of substrate capture, and rationalize the role of each component in the utilisome.
PubMed: 37286596
DOI: 10.1038/s41586-023-06146-w
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.65 Å)
Structure validation

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon