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Structure paper

TitleActive conformation of the p97-p47 unfoldase complex.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 2640, Year 2022
Publish dateMay 12, 2022
AuthorsYang Xu / Han Han / Ian Cooney / Yuxuan Guo / Noah G Moran / Nathan R Zuniga / John C Price / Christopher P Hill / Peter S Shen /
PubMed AbstractThe p97 AAA+ATPase is an essential and abundant regulator of protein homeostasis that plays a central role in unfolding ubiquitylated substrates. Here we report two cryo-EM structures of human p97 in ...The p97 AAA+ATPase is an essential and abundant regulator of protein homeostasis that plays a central role in unfolding ubiquitylated substrates. Here we report two cryo-EM structures of human p97 in complex with its p47 adaptor. One of the conformations is six-fold symmetric, corresponds to previously reported structures of p97, and lacks bound substrate. The other structure adopts a helical conformation, displays substrate running in an extended conformation through the pore of the p97 hexamer, and resembles structures reported for other AAA unfoldases. These findings support the model that p97 utilizes a "hand-over-hand" mechanism in which two residues of the substrate are translocated for hydrolysis of two ATPs, one in each of the two p97 AAA ATPase rings. Proteomics analysis supports the model that one p97 complex can bind multiple substrate adaptors or binding partners, and can process substrates with multiple types of ubiquitin modification.
External linksNat Commun / PubMed:35552390 / PubMed Central
MethodsEM (single particle)
Resolution3.6 - 5.7 Å
Structure data

23835

7mhs

EMDB-23835: Structure of p97 with substrate engaged
PDB-7mhs: Structure of p97 (subunits A to E) with substrate engaged
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-26654: Wild Type p97-p47 complex (symmetric hexamer)
Method: EM (single particle) / Resolution: 5.7 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE / p97 / VCP / AAA+ ATPase / peptide translocation

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