Abstract
AAA ATPases play central roles in cellular activities. The ATPase p97, a prototype of this superfamily, participates in organelle membrane fusion. Cryoelectron microscopy and single-particle analysis revealed that a major conformational change of p97 during the ATPase cycle occurred upon nucleotide binding and not during hydrolysis as previously hypothesized. Furthermore, our study indicates that six p47 adaptor molecules bind to the periphery of the ring-shaped p97 hexamer. Taken together, these results provide a revised model of how this and possibly other AAA ATPases can translate nucleotide binding into conformational changes of associated binding partners.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Diphosphate / metabolism
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Adenosine Triphosphatases / chemistry*
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Adenosine Triphosphatases / metabolism*
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Adenosine Triphosphatases / ultrastructure
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Adenosine Triphosphate / metabolism*
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Adenylyl Imidodiphosphate / metabolism
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Animals
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Carrier Proteins / chemistry
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Carrier Proteins / ultrastructure
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Cattle
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Cryoelectron Microscopy
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Image Processing, Computer-Assisted
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Membrane Proteins / metabolism
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Mice
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Models, Molecular
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N-Ethylmaleimide-Sensitive Proteins
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Nuclear Proteins / chemistry*
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Nuclear Proteins / metabolism*
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Nuclear Proteins / ultrastructure
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Protein Binding
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Protein Conformation
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SNARE Proteins
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Vesicular Transport Proteins*
Substances
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Carrier Proteins
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Membrane Proteins
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Nuclear Proteins
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SNARE Proteins
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Vesicular Transport Proteins
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Adenylyl Imidodiphosphate
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Adenosine Diphosphate
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Adenosine Triphosphate
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Adenosine Triphosphatases
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p97 ATPase
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N-Ethylmaleimide-Sensitive Proteins
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Nsf protein, mouse