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TitleCryo-electron microscopy structures of VCP/p97 reveal a new mechanism of oligomerization regulation.
Journal, issue, pagesiScience, Vol. 24, Issue 11, Page 103310, Year 2021
Publish dateNov 19, 2021
AuthorsGuimei Yu / Yunpeng Bai / Kunpeng Li / Ovini Amarasinghe / Wen Jiang / Zhong-Yin Zhang /
PubMed AbstractVCP/p97 is an evolutionarily conserved AAA+ ATPase important for cellular homeostasis. Previous studies suggest that VCP predominantly exists as a homohexamer. Here, we performed structural and ...VCP/p97 is an evolutionarily conserved AAA+ ATPase important for cellular homeostasis. Previous studies suggest that VCP predominantly exists as a homohexamer. Here, we performed structural and biochemical characterization of VCP dodecamer, an understudied state of VCP. The structure revealed an apo nucleotide status that has rarely been captured, a tail-to-tail assembly of two hexamers, and the up-elevated N-terminal domains akin to that seen in the ATP-bound hexamer. Further analyses elucidated a nucleotide status-dependent dodecamerization mechanism, where nucleotide dissociation from the D2 AAA domains induces and promotes VCP dodecamerization. In contrast, nucleotide-free D1 AAA domains are associated with the up-rotation of N-terminal domains, which may prime D1 for ATP binding. These results therefore reveal new nucleotide status-dictated intra- and interhexamer conformational changes and suggest that modulation of D2 domain nucleotide occupancy may serve as a mechanism in controlling VCP oligomeric states.
External linksiScience / PubMed:34765927 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 4.2 Å
Structure data

22675

7k56

EMDB-22675, PDB-7k56:
Structure of VCP dodecamer purified from H1299 cells
Method: EM (single particle) / Resolution: 3.9 Å

22676

7k57

EMDB-22676, PDB-7k57:
Structure of apo VCP dodecamer generated from bacterially recombinant VCP/p97
Method: EM (single particle) / Resolution: 3.7 Å

22678

7k59

EMDB-22678, PDB-7k59:
Structure of apo VCP hexamer generated from bacterially recombinant VCP/p97
Method: EM (single particle) / Resolution: 4.2 Å

Source
  • homo sapiens (human)
KeywordsCYTOSOLIC PROTEIN / HYDROLASE / AAA ATPase / ATP hydrolysis / segregase

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