ArticleCommunications biology2025
A new class of binding-protein dependent solute transporter exemplified by the TAXI-GltS system from Bordetella pertussis.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
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6 authors.
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Abstract
Tripartite ATP-independent periplasmic (TRAP) transporters are widespread in prokaryotes, but absent in eukaryotes, and transport various substrates. TRAP transporters are typically composed of a monomeric substrate binding protein (SBP) and a characteristic transmembrane component. Here, we describe the discovery and characterisation of a TRAP SBP from the TAXI subfamily with a previously unidentified architecture. BP0403 from Bordetella pertussis is a predicted lipoprotein with 3 distinct domains; an α/β globular domain, a helical domain and a C-terminal TAXI SBP domain. Characterisation of full-length BP0403 reveals that it forms a stable dimer, and structural modelling coupled with molecular weight analysis reveals that the interdomain helical region is solely responsible for dimerisation. Differential scanning fluorimetry (DSF) and intrinsic tyrosine fluorescence reveal that BP0403 binds L-glutamate with nanomolar affinity. Unexpectedly, genome context analysis of BP0403 reveals no TRAP membrane component genes; instead, we find co-localisation and translational coupling with gltS, encoding a Na
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