Author response: Conformational and dynamic plasticity in substrate-binding proteins underlies selective transport in ABC importers

Boer, Marijn de; Gouridis, Giorgos; Vietrov, Ruslan; Begg, Stephanie L.; Schuurman-Wolters, Gea K.; Husada, Florence; Eleftheriadis, Nikolaos; Poolman, Bert; McDevitt, Christopher A.; Cordes, Thorben

doi:10.7554/elife.44652.037

Cited by 2 publications

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“…Recently, it has been shown that SBPs can adopt a wide range of conformations that can activate transport and that both transported and non-transported ligands can adopt similar conformations in solution. While the SBP is the primary specificity determinant for the target molecule, it is suggested that the fate of the transported ligand can also be determined by selectivity at the membrane domain, or by a slow opening of the SBP, preventing translocation (de Boer et al, 2019). In both situations, it is clear that the docking and allosteric interaction of these domains is key in the transport cycle.…”

Section: Current Models For Protein:protein Interactions At the Membranementioning

confidence: 99%

Selective Nutrient Transport in Bacteria: Multicomponent Transporter Systems Reign Supreme

Davies

Currie

Wright

et al. 2021

Front. Mol. Biosci.

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Multicomponent transporters are used by bacteria to transport a wide range of nutrients. These systems use a substrate-binding protein to bind the nutrient with high affinity and then deliver it to a membrane-bound transporter for uptake. Nutrient uptake pathways are linked to the colonisation potential and pathogenicity of bacteria in humans and may be candidates for antimicrobial targeting. Here we review current research into bacterial multicomponent transport systems, with an emphasis on the interaction at the membrane, as well as new perspectives on the role of lipids and higher oligomers in these complex systems.

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Section: Current Models For Protein:protein Interactions At the Membranementioning

confidence: 99%

Selective Nutrient Transport in Bacteria: Multicomponent Transporter Systems Reign Supreme

Davies

Currie

Wright

et al. 2021

Front. Mol. Biosci.

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Substrate recognition and ATPase activity of the E. coli cysteine/cystine ABC transporter YecSC-FliY

Sabrialabed

Yang

Yariv

et al. 2020

Journal of Biological Chemistry

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Sulfur is essential for biological processes such as amino acid biogenesis, iron–sulfur cluster formation, and redox homeostasis. To acquire sulfur-containing compounds from the environment, bacteria have evolved high-affinity uptake systems, predominant among which is the ABC transporter family. Theses membrane-embedded enzymes use the energy of ATP hydrolysis for transmembrane transport of a wide range of biomolecules against concentration gradients. Three distinct bacterial ABC import systems of sulfur-containing compounds have been identified, but the molecular details of their transport mechanism remain poorly characterized. Here we provide results from a biochemical analysis of the purified Escherichia coli YecSC-FliY cysteine/cystine import system. We found that the substrate-binding protein FliY binds l-cystine, l-cysteine, and d-cysteine with micromolar affinities. However, binding of the l- and d-enantiomers induced different conformational changes of FliY, where the l- enantiomer–substrate-binding protein complex interacted more efficiently with the YecSC transporter. YecSC had low basal ATPase activity that was moderately stimulated by apo FliY, more strongly by d-cysteine–bound FliY, and maximally by l-cysteine– or l-cystine–bound FliY. However, at high FliY concentrations, YecSC reached maximal ATPase rates independent of the presence or nature of the substrate. These results suggest that FliY exists in a conformational equilibrium between an open, unliganded form that does not bind to the YecSC transporter and closed, unliganded and closed, liganded forms that bind this transporter with variable affinities but equally stimulate its ATPase activity. These findings differ from previous observations for similar ABC transporters, highlighting the extent of mechanistic diversity in this large protein family.

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Author response: Conformational and dynamic plasticity in substrate-binding proteins underlies selective transport in ABC importers

Cited by 2 publications

References 0 publications

Selective Nutrient Transport in Bacteria: Multicomponent Transporter Systems Reign Supreme

Selective Nutrient Transport in Bacteria: Multicomponent Transporter Systems Reign Supreme

Substrate recognition and ATPase activity of the E. coli cysteine/cystine ABC transporter YecSC-FliY

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