1E32

Structure of the N-Terminal domain and the D1 AAA domain of membrane fusion ATPase p97

Summary for 1E32

• Entry DOI: 10.2210/pdb1e32/pdb
• Descriptor: P97, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: atpase, membrane fusion
• Biological source: MUS MUSCULUS (HOUSE MOUSE)
• Total number of polymer chains: 1
• Total formula weight: 51454.68

Authors

Zhang, X.,Shaw, A.,Bates, P.A.,Gorman, M.A.,Kondo, H.,Dokurno, P.,Leonard M, G.,Sternberg, J.E.,Freemont, P.S. (deposition date: 2000-06-05, release date: 2001-05-31, Last modification date: 2024-05-08)

Primary citation

Zhang, X.,Shaw, A.,Bates, P.A.,Newman, R.H.,Gowen, B.,Orlova, E.,Gorman, M.A.,Kondo, H.,Dokurno, P.,Lally, J.,Leonard, G.,Meyer, H.,Van Heel, M.,Freemont, P.S.
Structure of the Aaa ATPase P97
Mol.Cell, 6:1473-, 2000

PubMed 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.

PubMed: 11163219
DOI: 10.1016/S1097-2765(00)00143-X

Experimental method

X-RAY DIFFRACTION (2.9 Å)