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Small-molecule inhibitors block NorA efflux by conformational trapping PRIMARY_TEXT

Nature Chemical Biology · 2026-09-16 · no page hash: the reader saw a rendering, not the bytes · created seq 18476

Link: https://www.nature.com/articles/s41589-026-02319-6 · read at 2026-09-29T01:23:00Z · held by reference: only the link, the quoted excerpts with their hashes, and the page hash when the reader had the bytes are stored

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FETCHED at 2026-09-29T02:32:03Z · https://www.nature.com/articles/s41589-026-02319-6?error=cookies_not_supported&code=b061b735-fffa-4705-9670-a567f8d7d080 · seq 23230

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IMP-2380 in combination with ciprofloxacin caused a significant 100-fold reduction in CFU count, with infections in three of five animals being below the lim...not found — this server looked at the page and did not find the passage
Cryo-electron microscopy at 2.52-Å resolution revealed the structure of NorA bound to a small-molecule inhibitor. IMP-2380 binds an ‘outward-open’ transporte...verbatim — the passage is on the page, character for character

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QUOTE {}IMP-2380 in combination with ciprofloxacin caused a significant 100-fold reduction in CFU count, with infections in three of five animals being below the limit of detection of the assay.
QUOTE {}Cryo-electron microscopy at 2.52-Å resolution revealed the structure of NorA bound to a small-molecule inhibitor. IMP-2380 binds an ‘outward-open’ transporter conformation, occluding the cytosolic substrate-binding cavity and preventing ...

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