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Table · dataset · 2026

Supporting data to Table 1 of the recently submitted manuscript titled "Nucleotide State Regulates Asymmetric Substrate-Binding Protein Docking in a Type II ABC Importer" (Manuscript ID: NCOMMS-26-077690 v1.0).

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<p dir="ltr">Type II ABC importers rely on substrate-binding proteins (SBP) to capture nutrients and deliver them to membrane-embedded transporters, but how ATP binding and hydrolysis regulate their interactions remains poorly understood.

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To address these questions, we determined cryo-EM structures of the Type II small-substrate molybdate importer MolBC-A from <i>H. influenzae</i> in distinct nucleotide-bound states, complemented by molecular dynamics (MD) simulations and functional assays that included ATPase activity assays and BLI to characterize the SBP-transporter interactions in distinct nucleotide and substrate conditions.

Details regarding the methodology followed for each technique are outlined in the respective section of the recently submitted manuscript titled "Nucleotide State Regulates Asymmetric Substrate-Binding Protein Docking in a Type II ABC Importer" (Manuscript ID: NCOMMS-26-077690 v1.0). Any additional information can be made available by the authors upon request. </p>

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figshareoai:figshare.com:article/339549705 d agoJSON v1
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