{
  "abstract": "How ATP binding and hydrolysis directionally reshape the conformational landscape remains unknown for ATP-binding cassette (ABC) transporters. Here, we identify two conserved ionic locks within the nucleotide-binding domains that govern transition barriers and energy transduction: an intra-subunit inward-facing (IF)-lock and an inter-subunit outward-facing (OF)-lock. Mg2+-ATP acts as a molecular key that disrupts the IF-lock, driving the forward transition. Following ATP hydrolysis, release of the {gamma}-phosphate, which, together with Mg2+, forms the pivot of the OF-lock, initiates the reverse transition. Directionality arises from kinetic asymmetry, driven by an anticorrelated exchange of the rate-limiting step between the consensus nucleotide-binding site and the transmembrane domains during forward and reverse transitions, respectively. Conservation of these molecular locks reveals a universal blueprint for ATP-driven mechanical transduction across the ABC superfamily.",
  "abstract_shown": true,
  "affiliations": [
    "Freie Universitaet Berlin"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 8,
  "authors": [
    {
      "name": "M. Rudolph"
    },
    {
      "name": "H. Batebi"
    },
    {
      "name": "M. Pramod"
    },
    {
      "name": "K. Barth"
    },
    {
      "name": "C. Hirschberg"
    },
    {
      "name": "R. Tampe"
    },
    {
      "name": "R. R. Netz"
    },
    {
      "affs": [
        0
      ],
      "name": "B. Joseph"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/7d720z4t73sh7.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.09.11.751009",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.09.11.751009v1.full",
  "id": "7d720z4t73sh7",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.09.11.751009v1",
  "language": null,
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biophysics"
    ],
    [
      "openalex",
      "2730|Drug Transport and Resistance Mechanisms"
    ]
  ],
  "openalex": "W7212454722",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.09.11.751009v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-11",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/7d720z4t73sh7.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:21:45Z",
      "native_id": "10.64898/2026.09.11.751009",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.09.11.751009v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:biophysics",
      "subfield": "biophysics"
    }
  ],
  "title": "Kinetic asymmetry drives directionality in an ATP-binding cassette transporter",
  "title_text": "Kinetic asymmetry drives directionality in an ATP-binding cassette transporter",
  "type": "preprint",
  "updated_at": "2026-10-30T12:21:45Z",
  "url": "https://research.draconitic.com/paper/7d720z4t73sh7",
  "venue": "bioRxiv",
  "versions": []
}