EMD-2590
Inter-ring rotations of AAA ATPase p97
EMD-2590
Single-particle20.0 Å
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Map released: 26/02/2014
Last modified: 19/03/2014
Sample Organism:
Mus musculus
Sample: p97 in presence of ADP, conformation 1
Deposition Authors: Yeung HO, Forster A
,
Bebeacua C,
Niwa H,
Ewens C,
McKeown C,
Zhang X
,
Freemont PS
Sample: p97 in presence of ADP, conformation 1
Deposition Authors: Yeung HO, Forster A
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Inter-ring rotations of AAA ATPase p97 revealed by electron cryomicroscopy
Yeung HO,
Forster A
,
Bebeacua C,
Niwa H,
Ewens C,
McKeown C,
Zhang X
,
Freemont PS
(2014) Open Biol , 4 , 130142 - 130142
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(2014) Open Biol , 4 , 130142 - 130142
Abstract:
The type II AAA+ protein p97 is involved in numerous cellular activities, including endoplasmic reticulum-associated degradation, transcription activation, membrane fusion and cell-cycle control. These activities are at least in part regulated by the ubiquitin system, in which p97 is thought to target ubiquitylated protein substrates within macromolecular complexes and assist in their extraction or disassembly. Although ATPase activity is essential for p97 function, little is known about how ATP binding or hydrolysis is coupled with p97 conformational changes and substrate remodelling. Here, we have used single-particle electron cryomicroscopy (cryo-EM) to study the effect of nucleotides on p97 conformation. We have identified conformational heterogeneity within the cryo-EM datasets from which we have resolved two major p97 conformations. A comparison of conformations reveals inter-ring rotations upon nucleotide binding and hydrolysis that may be linked to the remodelling of target protein complexes.
The type II AAA+ protein p97 is involved in numerous cellular activities, including endoplasmic reticulum-associated degradation, transcription activation, membrane fusion and cell-cycle control. These activities are at least in part regulated by the ubiquitin system, in which p97 is thought to target ubiquitylated protein substrates within macromolecular complexes and assist in their extraction or disassembly. Although ATPase activity is essential for p97 function, little is known about how ATP binding or hydrolysis is coupled with p97 conformational changes and substrate remodelling. Here, we have used single-particle electron cryomicroscopy (cryo-EM) to study the effect of nucleotides on p97 conformation. We have identified conformational heterogeneity within the cryo-EM datasets from which we have resolved two major p97 conformations. A comparison of conformations reveals inter-ring rotations upon nucleotide binding and hydrolysis that may be linked to the remodelling of target protein complexes.