Structure of the AAA ATPase p97

Xiaodong Zhang; Anthony Shaw; Paul A. Bates; Richard H. Newman; Brent Gowen; Elena Orlova; Michael A. Gorman; Hisao Kondo; Pawel Dokurno; John Lally; Gordon Leonard; Hemmo Meyer; Marin Van Heel; Paul S. Freemont

doi:10.1016/S1097-2765(00)00143-X

Structure of the AAA ATPase p97

Xiaodong Zhang, Anthony Shaw, Paul A. Bates, Richard H. Newman, Brent Gowen, Elena Orlova, Michael A. Gorman, Hisao Kondo, Pawel Dokurno, John Lally, Gordon Leonard, Hemmo Meyer, Marin Van Heel, Paul S. Freemont

Research output: Contribution to journal › Article › peer-review

379 Citations (Scopus)

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 routine p97 at 2.9 Å resolution, and a cryoelectron microscopy structure of full-length rat p97 at 18 Å resolution. Together, these structures show that the D1 and D2 hexamers pack in a tail-totail 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.

Original language	English
Pages (from-to)	1473-1484
Number of pages	12
Journal	Molecular Cell
Volume	6
Issue number	6
DOIs	https://doi.org/10.1016/S1097-2765(00)00143-X
Publication status	Published - 2000
Externally published	Yes

All Science Journal Classification (ASJC) codes

Molecular Biology
Cell Biology

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10.1016/S1097-2765(00)00143-X

Cite this

@article{bbf0ae4cbf794b95b992e03d529310bf,

title = "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 routine p97 at 2.9 {\AA} resolution, and a cryoelectron microscopy structure of full-length rat p97 at 18 {\AA} resolution. Together, these structures show that the D1 and D2 hexamers pack in a tail-totail 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.",

author = "Xiaodong Zhang and Anthony Shaw and Bates, {Paul A.} and Newman, {Richard H.} and Brent Gowen and Elena Orlova and Gorman, {Michael A.} and Hisao Kondo and Pawel Dokurno and John Lally and Gordon Leonard and Hemmo Meyer and {Van Heel}, Marin and Freemont, {Paul S.}",

year = "2000",

doi = "10.1016/S1097-2765(00)00143-X",

language = "English",

volume = "6",

pages = "1473--1484",

journal = "Molecular Cell",

issn = "1097-2765",

publisher = "Cell Press",

number = "6",

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TY - JOUR

T1 - Structure of the AAA ATPase p97

AU - Zhang, Xiaodong

AU - Shaw, Anthony

AU - Bates, Paul A.

AU - Newman, Richard H.

AU - Gowen, Brent

AU - Orlova, Elena

AU - Gorman, Michael A.

AU - Kondo, Hisao

AU - Dokurno, Pawel

AU - Lally, John

AU - Leonard, Gordon

AU - Meyer, Hemmo

AU - Van Heel, Marin

AU - Freemont, Paul S.

PY - 2000

Y1 - 2000

N2 - 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 routine p97 at 2.9 Å resolution, and a cryoelectron microscopy structure of full-length rat p97 at 18 Å resolution. Together, these structures show that the D1 and D2 hexamers pack in a tail-totail 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.

AB - 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 routine p97 at 2.9 Å resolution, and a cryoelectron microscopy structure of full-length rat p97 at 18 Å resolution. Together, these structures show that the D1 and D2 hexamers pack in a tail-totail 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.

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U2 - 10.1016/S1097-2765(00)00143-X

DO - 10.1016/S1097-2765(00)00143-X

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SN - 1097-2765

VL - 6

SP - 1473

EP - 1484

JO - Molecular Cell

JF - Molecular Cell

IS - 6

ER -

Structure of the AAA ATPase p97

Abstract

All Science Journal Classification (ASJC) codes

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