The crystal structure of murine p97/VCP at 3.6 Å

Trevor Huyton, Valerie E. Pye, Louise C. Briggs, Terence C. Flynn, Fabienne Beuron, Hisao Kondo, Jianpeng Ma, Xiaodong Zhang, Paul S. Freemont

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142 Citations (Scopus)


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 3.6Å crystal structure of murine p97 in which D2 domain has been modelled as poly-alanine and the remaining ~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.

Original languageEnglish
Pages (from-to)337-348
Number of pages12
JournalJournal of structural biology
Issue number3
Publication statusPublished - Dec 2003
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology

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    Huyton, T., Pye, V. E., Briggs, L. C., Flynn, T. C., Beuron, F., Kondo, H., Ma, J., Zhang, X., & Freemont, P. S. (2003). The crystal structure of murine p97/VCP at 3.6 Å. Journal of structural biology, 144(3), 337-348.