5VCA
VCP like ATPase from T. acidophilum (VAT)-Substrate bound conformation
Summary for 5VCA
| Entry DOI | 10.2210/pdb5vca/pdb |
| Related | 5VC7 |
| EMDB information | 8658 8659 |
| Descriptor | VCP-like ATPase (1 entity in total) |
| Functional Keywords | aaa+, atpase, complex, unfoldase, hydrolase |
| Biological source | Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) |
| Total number of polymer chains | 6 |
| Total formula weight | 377977.48 |
| Authors | Ripstein, Z.A.,Huang, R.,Augustyniak, R.,Kay, L.E.,Rubinstein, J.L. (deposition date: 2017-03-31, release date: 2017-04-26, Last modification date: 2024-11-06) |
| Primary citation | Ripstein, Z.A.,Huang, R.,Augustyniak, R.,Kay, L.E.,Rubinstein, J.L. Structure of a AAA+ unfoldase in the process of unfolding substrate. Elife, 6:-, 2017 Cited by PubMed Abstract: AAA+ unfoldases are thought to unfold substrate through the central pore of their hexameric structures, but how this process occurs is not known. VAT, the homologue of eukaryotic CDC48/p97, works in conjunction with the proteasome to degrade misfolded or damaged proteins. We show that in the presence of ATP, VAT with its regulatory N-terminal domains removed unfolds other VAT complexes as substrate. We captured images of this transient process by electron cryomicroscopy (cryo-EM) to reveal the structure of the substrate-bound intermediate. Substrate binding breaks the six-fold symmetry of the complex, allowing five of the six VAT subunits to constrict into a tight helix that grips an ~80 Å stretch of unfolded protein. The structure suggests a processive hand-over-hand unfolding mechanism, where each VAT subunit releases the substrate in turn before re-engaging further along the target protein, thereby unfolding it. PubMed: 28390173DOI: 10.7554/eLife.25754 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.8 Å) |
Structure validation
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