Document Detail


Interprotomer motion-transmission mechanism for the hexameric AAA ATPase p97.
MedLine Citation:
PMID:  22355145     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Multimeric AAA ATPases represent a structurally homologous yet functionally diverse family of proteins. The essential and highly abundant hexameric AAA ATPase p97 is perhaps the best studied AAA protein, playing an essential role in various important cellular activities. During ATP-hydrolysis process, p97 undergoes dramatic conformational changes, and these changes are initiated in the C-terminal ATPase domain and transmitted across the entire length of the molecule to the N-terminal effector domain. However, the detailed mechanism of the motion transmission remains unclear. Here, we report an interprotomer motion-transmission mechanism to explain this process: The nucleotide-dependent motion transmission between the two ATPase domains of one protomer is mediated by its neighboring protomer. This finding reveals a strict requirement for interprotomer coordination of p97 during the motion-transmission process and may shed light on studies of other AAA ATPases.
Authors:
Guangtao Li; Chengdong Huang; Gang Zhao; William J Lennarz
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-02-21
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  109     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2012 Mar 
Date Detail:
Created Date:  2012-03-07     Completed Date:  2012-05-04     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3737-41     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / chemistry*,  physiology
Adenosine Triphosphate / chemistry
Animals
Cell Separation
Endoplasmic Reticulum / metabolism
Flow Cytometry
HEK293 Cells
Humans
Hydrolysis
Mice
Models, Molecular
Molecular Conformation
Motion
Mutation
Nuclear Proteins / chemistry*,  physiology
Nucleotides / chemistry
Protein Conformation
Protein Structure, Tertiary
Grant Support
ID/Acronym/Agency:
GM33814/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Nuclear Proteins; 0/Nucleotides; 56-65-5/Adenosine Triphosphate; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/p97 ATPase
Comments/Corrections

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