B. Van Den Berg
University of Oxford
14 Papers
83 Citations
B. Van Den Berg is an academic researcher from University of Oxford. The author has contributed to research in topics: Biology & Bacterial outer membrane. The author has an hindex of 1, co-authored 1 publications.
Chat about Author
Papers
Characterisation of the dominant oxidative folding intermediate of hen lysozyme.
TL;DR: Characterisation of des-[76-94] by 2D1H NMR shows that it has a highly native-like structure, which provides an explanation for the accumulation of this species during refolding as direct oxidation to the fully native protein will be restricted by the burial of Cys94 in the protein interior.
84
TonB-Dependent Transport Across the Bacterial Outer Membrane.
TL;DR: TonB-dependent transporters (TBDTs) are present in all gram-negative bacteria and mediate energy-dependent uptake of molecules that are too scarce or large to be taken up efficiently by outer membrane (OM) diffusion channels as mentioned in this paper .
38
Outer membrane utilisomes mediate glycan uptake in gut Bacteroidetes
Joshua B. R. White,Augustinas Silale,M Feasey,Tiaan Heunis,Yiling Zhu,Hongwu Zheng,Akshada Gajbhiye,Susan J. Firbank,Arnaud Baslé,Matthias Trost,David N. Bolam,B. Van Den Berg,Neil A. Ranson +12 more
TL;DR: It is shown 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 the authors term utilisomes.
24
Structural basis for host recognition and superinfection exclusion by bacteriophage T5
TL;DR: The cryo-EM structure of the phage T5 outer membrane (OM) receptor FhuA in complex with the T5 RBP pb5, and the crystal structure of Fhu a complexed to the OM SE lipoprotein Llp reveals that Llp is periplasmic and binds to a non-native conformation of the plug of F HuA, causing the inward folding of two extracellular loops via “reverse” allostery.
18
Gut Commensal Bacteroidetes Encode a Novel Class of Vitamin B12-Binding Proteins
Emily E. Putnam,Javier Abellón-Ruiz,Bryan J. Killinger,Joshua J. Rosnow,Aaron G. Wexler,Ewa Folta-Stogniew,Aaron T. Wright,B. Van Den Berg,Andrew L. Goodman +8 more
TL;DR: A new protein is identified, BtuH, which binds vitamin B12 directly via a C-terminal globular domain that has no known structural homologs, demonstrating that members of the heterogeneous suite of accessory proteins encoded in Bacteroides cobamide transport system loci can play key roles in vitamin acquisition.