The crystal structure of murine p97/VCP at 3.6A.
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 3.6A crystal structure of murine p97 in which D2 domain has been modelled as poly-alanine and the remaining approximately 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.
Huyton
Trevor
T
Department of Biological Sciences, Imperial College London, South Kensington SW7 2AZ, UK.
Pye
Valerie E
VE
Briggs
Louise C
LC
Flynn
Terence C
TC
Beuron
Fabienne
F
Kondo
Hisao
H
Ma
Jianpeng
J
Zhang
Xiaodong
X
Freemont
Paul S
PS
D000251:Adenosine Triphosphatases / Q000737:chemistry; D000818:Animals; D016880:Anisotropy; D018797:Cell Cycle Proteins / Q000737:chemistry*; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004583:Electrons; D049071:Endopeptidase Clp; D051379:Mice; D008958:Models, Molecular; D015233:Models, Statistical; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry; D000074405:Valosin Containing Protein
D018797:Cell Cycle Proteins; D011994:Recombinant Proteins; D012697:Serine Endopeptidases; D049071:Endopeptidase Clp; D000251:Adenosine Triphosphatases; D000074405:Valosin Containing Protein; C000614179:Vcp protein, mouse