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Journal Article

Nucleotide-dependent conformational changes of the AAA+ ATPase p97 revisited

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Schuller,  Jan M.
Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society;

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Beck,  Florian
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Förster,  Friedrich
Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Schuller, J. M., Beck, F., Lossl, P., Heck, A. J. R., & Förster, F. (2016). Nucleotide-dependent conformational changes of the AAA+ ATPase p97 revisited. FEBS LETTERS, 590(5), 595-604. doi:10.1002/1873-3468.12091.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-2BFB-2
Abstract
The ubiquitous AAA-ATPase p97 segregates ubiquitylated proteins from their molecular environment. Previous studies of the nucleotide-dependent conformational changes of p97 were inconclusive. Here, we determined its structure in the presence of ADP, AMP-PNP, or ATP-gamma S at 6.1-7.4 angstrom resolution using single particle cryo-electron microscopy. Both AAA domains, D1 and D2, assemble into essentially six-fold symmetrical rings. The pore of the D1-ring remains essentially closed under all nucleotide conditions, whereas the D2-ring shows an iris-like opening for ADP. The largest conformational changes of p97 are 'swinging motions' of the N-terminal domains, which may enable segregation of ubiquitylated substrates from their environment.