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Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle
Isabelle Rouiller1, Byron DeLaBarre, Andrew P May
1The Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
Nature Structural Biology
|November 16, 2002
Summary
The AAA ATPase p97 (VCP) undergoes significant conformational changes during its ATPase cycle. These movements involve domain rotation and fluctuating openings, crucial for its cellular functions.
Area of Science:
- Molecular Biology
- Biochemistry
- Cell Biology
Background:
- p97 (VCP) is an AAA ATPase vital for cellular functions like membrane fusion and protein degradation.
- Understanding its mechanism requires detailed analysis of its dynamic conformational changes.
Purpose of the Study:
- To investigate the conformational dynamics of p97 (VCP) throughout its ATPase cycle.
- To elucidate the structural basis of p97 (VCP) function at a molecular level.
Main Methods:
- Cryo-electron microscopy (cryo-EM) was employed.
- Single-particle analysis was used to generate 3D maps.
Main Results:
- Conformational changes were observed in the N-domains, D1, and D2 AAA domains during ATP binding, hydrolysis, and nucleotide release.
- The N-domain exhibits flexibility, becoming rigid post-ATP hydrolysis.
- The D1 and D2 rings rotate relative to each other, with dynamic axial opening sizes.
Conclusions:
- The study provides a detailed depiction of the movements within p97 (VCP) during its ATPase cycle.
- These findings offer insights into the mechanism of p97 (VCP) and potentially other AAA ATPases.