| The crystal structure of murine p97/VCP at 3.6A. | |
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MedLine Citation:
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PMID: 14643202 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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p97/VCP is a member of the AAA ATPase family and has roles in both membrane fusion and ubiquitin dependent protein degradation. Here, we present a 3.6A crystal structure of murine p97 in which D2 domain has been modelled as poly-alanine and the remaining approximately 100 residues are absent. The resulting structure illustrates a head-to-tail packing arrangement of the two p97 AAA domains in a natural hexameric state with D1 ADP bound and D2 nucleotide free. The head-to-tail packing arrangement observed in this structure is in contrast to our previously predicted tail-to-tail packing model. The linker between the D1 and D2 domains is partially disordered, suggesting a flexible nature. Normal mode analysis of the crystal structure suggests anti-correlated motions and distinct conformational states of the two AAA domains. |
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Authors:
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Trevor Huyton; Valerie E Pye; Louise C Briggs; Terence C Flynn; Fabienne Beuron; Hisao Kondo; Jianpeng Ma; Xiaodong Zhang; Paul S Freemont |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Journal of structural biology Volume: 144 ISSN: 1047-8477 ISO Abbreviation: J. Struct. Biol. Publication Date: 2003 Dec |
Date Detail:
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Created Date: 2003-12-03 Completed Date: 2004-07-19 Revised Date: 2009-09-03 |
Medline Journal Info:
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Nlm Unique ID: 9011206 Medline TA: J Struct Biol Country: United States |
Other Details:
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Languages: eng Pagination: 337-48 Citation Subset: IM |
Affiliation:
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Department of Biological Sciences, Imperial College London, South Kensington SW7 2AZ, UK. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphatases
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chemistry Animals Anisotropy Cell Cycle Proteins / chemistry* Cloning, Molecular Crystallography, X-Ray Electrons Endopeptidase Clp Mice Models, Molecular Models, Statistical Protein Conformation Protein Structure, Tertiary Recombinant Proteins / chemistry Serine Endopeptidases / chemistry |
| Grant Support | |
ID/Acronym/Agency:
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R01-GM067801/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Cell Cycle Proteins; 0/Recombinant Proteins; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.92/Endopeptidase Clp; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/CDC48 protein |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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