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TitleNucleotide-dependent conformational changes of the AAA+ ATPase p97 revisited.
Journal, issue, pagesFEBS Lett, Vol. 590, Issue 5, Page 595-604, Year 2016
Publish dateFeb 20, 2016
AuthorsJan M Schuller / Florian Beck / Philip Lössl / Albert J R Heck / Friedrich Förster /
PubMed AbstractThe 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 linksFEBS Lett / PubMed:26849035
MethodsEM (single particle)
Resolution6.1 - 9.3 Å
Structure data

EMDB-3323:
p97 in the ADP state C6 symmetrized
Method: EM (single particle) / Resolution: 6.9 Å

EMDB-3324:
p97 in the AMPPNP state C6 symmetrized
Method: EM (single particle) / Resolution: 7.5 Å

EMDB-3325:
p97 in the ATPyS state C6 symmetrized
Method: EM (single particle) / Resolution: 6.1 Å

EMDB-3326:
p97 in the ADP state no symmetry applied
Method: EM (single particle) / Resolution: 9.0 Å

EMDB-3327:
p97 in the ATPyS state, no symmetry applied
Method: EM (single particle) / Resolution: 8.1 Å

EMDB-3328:
p97 in the AMPPNP state, no symmetry applied
Method: EM (single particle) / Resolution: 9.3 Å

Source
  • Homo sapiens (human)

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