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Title | Nucleotide-dependent conformational changes of the AAA+ ATPase p97 revisited. |
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Journal, issue, pages | FEBS Lett, Vol. 590, Issue 5, Page 595-604, Year 2016 |
Publish date | Feb 20, 2016 |
Authors | Jan M Schuller / Florian Beck / Philip Lössl / Albert J R Heck / Friedrich Förster / |
PubMed 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, ...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-γS at 6.1-7.4 Å 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. |
External links | FEBS Lett / PubMed:26849035 |
Methods | EM (single particle) |
Resolution | 6.1 - 9.3 Å |
Structure data | EMDB-3323: EMDB-3324: EMDB-3325: EMDB-3326: EMDB-3327: EMDB-3328: |
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