Functional and structural characterization of an ECF-type ABC transporter for vitamin B12

Luís da Silva Santos Guimarães, J. A., Rempel, S., Mous, S. T. M., Tambascia Pereira, C., ter Beek, J., Gier, J-W. D., Guskov, A. & Slotboom, D., 2018, In : eLife. 7, 16 p., e35828.

Research output: Contribution to journalArticleAcademicpeer-review

  • Joana Abreu Luís da Silva Santos Guimarães
  • Stephan Rempel
  • Sandra Tecla Ma Mous
  • Cristiane Tambascia Pereira
  • Josy ter Beek
  • Jan-Willem de Gier
  • Albert Guskov
  • Dirk Slotboom
Vitamin B12 (cobalamin) is the most complex B-type vitamin and is synthetized exclusively in a limited number of prokaryotes. Its biologically active variants contain rare organometallic bonds, which are used by enzymes in a variety of central metabolic pathways such as L-methionine synthesis and ribonucleotide reduction. Although its biosynthesis and role as co-factor are well understood, knowledge about uptake of cobalamin by prokaryotic auxotrophs is scarce. Here, we characterize a cobalamin-specific ECF-type ABC transporter from Lactobacillus delbrueckii, ECF-CbrT, and demonstrate that it mediates the specific, ATP-dependent uptake of cobalamin. We solved the crystal structure of ECF-CbrT in an apo conformation to 3.4 Å resolution. Comparison with the ECF transporter for folate (ECF-FolT2) from the same organism, reveals how the identical ECF module adjusts to interact with the different substrate binding proteins FolT2 and CbrT. ECF-CbrT is unrelated to the well-characterized B12 transporter BtuCDF, but their biochemical features indicate functional convergence.
Original languageEnglish
Article numbere35828
Number of pages16
Publication statusPublished - 2018

Download statistics

No data available

ID: 61205517