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Functional and structural characterization of an ECF-type ABC transporter for vitamin B12
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Number of Authors: 82018 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 7, article id e35828Article in journal (Refereed) Published
Abstract [en]

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 cofactor 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 angstrom resolution. Comparison with the ECF transporter for folate (ECF-FoIT2) from the same organism, reveals how the identical ECF module adjusts to interact with the different substrate binding proteins FoIT2 and CbrT. ECF-CbrT is unrelated to the well-characterized B12 transporter BtuCDF, but their biochemical features indicate functional convergence.

Place, publisher, year, edition, pages
2018. Vol. 7, article id e35828
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Biological Sciences
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URN: urn:nbn:se:su:diva-158194DOI: 10.7554/eLife.35828ISI: 000435002300001PubMedID: 29809140OAI: oai:DiVA.org:su-158194DiVA, id: diva2:1234210
Available from: 2018-07-23 Created: 2018-07-23 Last updated: 2018-07-23Bibliographically approved

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Rempel, Stephanter Beek, Josyde Gier, Jan-WillemGuskov, Albert
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Department of Biochemistry and Biophysics
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