IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v16y2025i1d10.1038_s41467-025-61962-0.html
   My bibliography  Save this article

ATP plays a structural role in Hsp90 function

Author

Listed:
  • Michael Reidy

    (National Institutes of Health)

  • Daniel C. Masison

    (National Institutes of Health)

Abstract

Hsp90 is a highly conserved ATP-dependent molecular chaperone that forms a clamp around client proteins. The role of ATP in Hsp90 function is unclear since cell viability requires ATP binding, but not hydrolysis. Here, we present findings that support our hypothesis that after ATP binds, the γ phosphate repositions in a regulated manner to interact with a conserved arginine (R380) and stabilize the closed clamp. We propose that the essential role of ATP in Hsp90 function is structural: ATP is a linker that physically tethers the N and M domains and stabilizes closing. Severing this link by hydrolysis facilitates reopening. Our findings support the idea that R380 is an arginine finger, a motif found in diverse NTPase families, due to its interdomain interaction with ATP. This in turn suggests that for some arginine fingers the nucleotide itself is a structural element important for stabilization of inter-domain or -subunit interactions.

Suggested Citation

  • Michael Reidy & Daniel C. Masison, 2025. "ATP plays a structural role in Hsp90 function," Nature Communications, Nature, vol. 16(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-61962-0
    DOI: 10.1038/s41467-025-61962-0
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-025-61962-0
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-025-61962-0?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-61962-0. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.