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ATP plays a structural role in Hsp90 function.

Michael Reidy1, Daniel C Masison2

  • 1Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA. michael.reidy@nih.gov.

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Summary

Adenosine triphosphate (ATP) binding, not hydrolysis, is essential for Hsp90 chaperone function. ATP acts as a structural linker, stabilizing the Hsp90 clamp through interactions with arginine R380.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Heat shock protein 90 (Hsp90) is a crucial molecular chaperone.
  • Hsp90 utilizes adenosine triphosphate (ATP) for its function.
  • The precise role of ATP binding versus hydrolysis in Hsp90's mechanism remains unclear.

Purpose of the Study:

  • To elucidate the structural role of ATP in Hsp90 chaperone function.
  • To investigate the interaction between ATP and conserved residues, specifically arginine R380.
  • To understand how ATP binding and hydrolysis influence Hsp90 clamp dynamics.

Main Methods:

  • The study likely involved structural biology techniques (e.g., X-ray crystallography, cryo-EM) to visualize Hsp90-ATP complexes.
  • Biochemical assays were probably used to assess the impact of ATP binding and hydrolysis on Hsp90 activity.
  • Mutagenesis studies targeting R380 may have been employed to test its functional significance.

Main Results:

  • Findings indicate that ATP binding, not hydrolysis, is critical for Hsp90's structural integrity and function.
  • The gamma phosphate of ATP repositions to interact with arginine R380, stabilizing the closed chaperone clamp.
  • ATP acts as a structural linker, tethering the N and M domains of Hsp90, with hydrolysis facilitating clamp reopening.

Conclusions:

  • The essential role of ATP in Hsp90 function is structural, serving to stabilize the closed clamp conformation.
  • Arginine R380 functions as an "arginine finger" by interacting with ATP, suggesting nucleotides can be structural elements in NTPase families.
  • This work provides new insights into the mechanism of Hsp90 and the broader role of nucleotides in protein-ligand interactions.