ArticleScientific reports2017
Conformational Change of a Tryptophan Residue in BtuF Facilitates Binding and Transport of Cobinamide by the Vitamin B12 Transporter BtuCD-F.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- Cobamide Scavenging and Import via a Multiprotein Extracellular Relay in Bacteroides thetaiotaomicron.Chembiochem : a European journal of chemical biology · 2026Review
- The Antidepressant Drug Clomipramine Inhibits the ABC Transporter BmrA.Chembiochem : a European journal of chemical biology · 2026Article
- Ligand cross-feeding resolves bacterial vitamin BNature · 2024Article
- Bidirectional ATP-driven transport of cobalamin by the mycobacterial ABC transporter BacA.Nature communications · 2024Article
- Sharing vitamins: Cobamides unveil microbial interactions.Science (New York, N.Y.) · 2020Review
- Flexible Cobamide Metabolism inJournal of bacteriology · 2020Article
- The Different Effects of Substrates and Nucleotides on the Complex Formation of ABC Transporters.Structure (London, England : 1993) · 2019Article
- Functional and structural characterization of an ECF-type ABC transporter for vitamin B12.eLife · 2018Article
- Single-molecule visualization of conformational changes and substrate transport in the vitamin BNature communications · 2017Article
- Structural basis of nanobody-mediated blocking of BtuF, the cognate substrate-binding protein of the Escherichia coli vitamin B12 transporter BtuCD.Scientific reports · 2017Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BtuCD-F is an ABC transporter that mediates cobalamin uptake into Escherichia coli. Early in vivo data suggested that BtuCD-F might also be involved in the uptake of cobinamide, a cobalamin precursor. However, neither was it demonstrated that BtuCD-F indeed transports cobinamide, nor was the structural basis of its recognition known. We synthesized radiolabeled cyano-cobinamide and demonstrated BtuCD-catalyzed in vitro transport, which was ATP- and BtuF-dependent. The crystal structure of cobinamide-bound BtuF revealed a conformational change of a tryptophan residue (W66) in the substrate binding cleft compared to the structure of cobalamin-bound BtuF. High-affinity binding of cobinamide was dependent on W66, because mutation to most other amino acids substantially reduced binding. The structures of three BtuF W66 mutants revealed that tight packing against bound cobinamide was only provided by tryptophan and phenylalanine, in line with the observed binding affinities. In vitro transport rates of cobinamide and cobalamin were not influenced by the substitutions of BtuF W66 under the experimental conditions, indicating that W66 has no critical role in the transport reaction. Our data present the molecular basis of the cobinamide versus cobalamin specificity of BtuCD-F and provide tools for in vitro cobinamide transport and binding assays.
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