{
  "abstract": "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. To address these questions, we determined structures of the Type II small-substrate molybdate importer MolBC-A from H. influenzae in distinct nucleotide-bound states, complemented by molecular dynamics (MD) simulations and functional assays. In a nucleotide-free state, the MolA-MolBC interface is remodeled into a more open conformation, whereas ATP and AMP-PNP binding induce asymmetric conformational changes that preserve the MolA Lobe I interface and disrupt contacts with MolA Lobe II, revealing a previously unresolved partially-docked state. In the ADP-bound state, MolA exhibits the greatest conformational heterogeneity with reduced stable engagement that extends across both lobes. Together these findings define a nucleotide-dependent cycle of asymmetric MolA remodeling and reveal distinct contributions of the two SBP lobes in coupling transporter nucleotide state to SBP engagement.",
  "abstract_shown": true,
  "affiliations": [
    "Northwestern University"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 5,
  "authors": [
    {
      "name": "A. Karagiaridi"
    },
    {
      "name": "R. Mendoza Uriarte"
    },
    {
      "name": "M. Chen"
    },
    {
      "name": "B. Roux"
    },
    {
      "affs": [
        0
      ],
      "name": "H. W. Pinkett"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/avejggm5n7dz4.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.10.15.759412",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.10.15.759412v1.full",
  "id": "avejggm5n7dz4",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.10.15.759412v1",
  "language": null,
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biochemistry"
    ],
    [
      "openalex",
      "2730|Drug Transport and Resistance Mechanisms"
    ]
  ],
  "openalex": "W7222592033",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.10.15.759412v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-15",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/avejggm5n7dz4.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:28:07Z",
      "native_id": "10.64898/2026.10.15.759412",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.10.15.759412v1"
    }
  ],
  "subjects": [
    {
      "field": "medicine",
      "origin": "openalex:2730|Drug Transport and Resistance Mechanisms",
      "subfield": "oncology"
    }
  ],
  "title": "Nucleotide State Regulates Asymmetric Substrate-Binding Protein Docking in a Type II ABC Importer",
  "title_text": "Nucleotide State Regulates Asymmetric Substrate-Binding Protein Docking in a Type II ABC Importer",
  "type": "preprint",
  "updated_at": "2026-10-30T12:28:07Z",
  "url": "https://research.draconitic.com/paper/avejggm5n7dz4",
  "venue": "bioRxiv",
  "versions": []
}