A Major Conformational Change in p97 AAA ATPase upon ATP Binding

• Published in: Molecular cell Vol. 6; no. 6; pp. 1485 - 1490
• Main Authors: Rouiller, Isabelle, Butel, Virginia M, Latterich, Martin, Milligan, Ronald A, Wilson-Kubalek, Elizabeth M
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.12.2000
• Subjects: Adenosine Diphosphate - metabolism; Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - metabolism; Adenosine Triphosphatases - ultrastructure; Adenosine Triphosphate - metabolism; Adenylyl Imidodiphosphate - metabolism; Animals; Carrier Proteins - chemistry; Carrier Proteins - ultrastructure; Cattle; Cryoelectron Microscopy; Image Processing, Computer-Assisted; Membrane Proteins - metabolism; Mice; Models, Molecular; N-Ethylmaleimide-Sensitive Proteins; Nuclear Proteins - chemistry; Nuclear Proteins - metabolism; Nuclear Proteins - ultrastructure; Protein Binding; Protein Conformation; SNARE Proteins; Vesicular Transport Proteins
• ISSN: 1097-2765; 1097-4164
• DOI: 10.1016/S1097-2765(00)00144-1

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.