5G4G: Structure Of The Atpgs-bound Vat Complex

The AAA+ (ATPases associated with a variety of cellular activities) enzymes play critical roles in a variety of homeostatic processes in all kingdoms of life. Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), the archaeal homolog of the ubiquitous AAA+ protein Cdc48/p97, functions in concert with the 20S proteasome by unfolding substrates and passing them on for degradation. Here, we present electron cryomicroscopy (cryo-EM) maps showing that VAT undergoes large conformational rearrangements during its ATP hydrolysis cycle that differ dramatically from the conformational states observed for Cdc48/p97. We validate key features of the model with biochemical and solution methyl-transverse relaxation optimized spectroscopY (TROSY) NMR experiments and suggest a mechanism for coupling the energy of nucleotide hydrolysis to substrate unfolding. These findings illustrate the unique complementarity between cryo-EM and solution NMR for studies of molecular machines, showing that the structural properties of VAT, as well as the population distributions of conformers, are similar in the frozen specimens used for cryo-EM and in the solution phase where NMR spectra are recorded.
PDB ID: 5G4GDownload
MMDB ID: 141336
PDB Deposition Date: 2016/5/12
Updated in MMDB: 2016/08
Experimental Method:
electron microscopy
Resolution: 7.8  Å
Source Organism:
Similar Structures:
Biological Unit for 5G4G: hexameric; determined by software (PISA)
Molecular Components in 5G4G
Label Count Molecule
Proteins (6 molecules)
Vcp-like Atpase(Gene symbol: TA_RS04345)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB