Structure of the AAA ATPase p97
- PMID: 11163219
- DOI: 10.1016/s1097-2765(00)00143-x
Structure of the AAA ATPase p97
Abstract
p97, an abundant hexameric ATPase of the AAA family, is involved in homotypic membrane fusion. It is thought to disassemble SNARE complexes formed during the process of membrane fusion. Here, we report two structures: a crystal structure of the N-terminal and D1 ATPase domains of murine p97 at 2.9 A resolution, and a cryoelectron microscopy structure of full-length rat p97 at 18 A resolution. Together, these structures show that the D1 and D2 hexamers pack in a tail-to-tail arrangement, and that the N domain is flexible. A comparison with NSF D2 (ATP complex) reveals possible conformational changes induced by ATP hydrolysis. Given the D1 and D2 packing arrangement, we propose a ratchet mechanism for p97 during its ATP hydrolysis cycle.
Similar articles
-
A major conformational change in p97 AAA ATPase upon ATP binding.Mol Cell. 2000 Dec;6(6):1485-90. doi: 10.1016/s1097-2765(00)00144-1. Mol Cell. 2000. PMID: 11163220
-
Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle.Nat Struct Biol. 2002 Dec;9(12):950-7. doi: 10.1038/nsb872. Nat Struct Biol. 2002. PMID: 12434150
-
Conformational changes in the AAA ATPase p97-p47 adaptor complex.EMBO J. 2006 May 3;25(9):1967-76. doi: 10.1038/sj.emboj.7601055. Epub 2006 Apr 6. EMBO J. 2006. PMID: 16601695 Free PMC article.
-
NSF and p97/VCP: similar at first, different at last.FEBS Lett. 2003 Nov 27;555(1):126-33. doi: 10.1016/s0014-5793(03)01107-4. FEBS Lett. 2003. PMID: 14630332 Review.
-
N-ethylmaleimide sensitive factor (NSF) structure and function.Int Rev Cytol. 2001;207:71-112. doi: 10.1016/s0074-7696(01)07003-6. Int Rev Cytol. 2001. PMID: 11352269 Review.
Cited by
-
The Role of VCP Mutations in the Spectrum of Amyotrophic Lateral Sclerosis-Frontotemporal Dementia.Front Neurol. 2022 Feb 22;13:841394. doi: 10.3389/fneur.2022.841394. eCollection 2022. Front Neurol. 2022. PMID: 35273561 Free PMC article. Review.
-
Three semidominant barley mutants with single amino acid substitutions in the smallest magnesium chelatase subunit form defective AAA+ hexamers.Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13944-9. doi: 10.1073/pnas.212504499. Epub 2002 Sep 30. Proc Natl Acad Sci U S A. 2002. PMID: 12357035 Free PMC article.
-
The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment.EMBO J. 2006 May 3;25(9):1827-35. doi: 10.1038/sj.emboj.7601088. Epub 2006 Apr 13. EMBO J. 2006. PMID: 16619026 Free PMC article.
-
Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains.J Cell Biol. 2003 Jul 7;162(1):71-84. doi: 10.1083/jcb.200302169. J Cell Biol. 2003. PMID: 12847084 Free PMC article.
-
Hexameric ring structure of the full-length archaeal MCM protein complex.EMBO Rep. 2003 Nov;4(11):1079-83. doi: 10.1038/sj.embor.embor7400010. Epub 2003 Oct 17. EMBO Rep. 2003. PMID: 14566326 Free PMC article.
MeSH terms
Substances
Associated data
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
