in contrast to wild-type NFS E329Q mutant is enriched on various structures throughout the cell and is only minimally released by saponin permeabilization
naturally occurring mutation, constitutes variations in surface-exposed locations. The E219K mutation leads to an almost complete loss of activity, which is partially recuperated in the R154C/E219K double-mutant indicating p97 inter-domain communication
naturally occurring mutation, constitutes variations in surface-exposed locations and leads to increased ATPase activity, and a twofold decreased kd for human protein UBXD9
naturally occurring mutation, constitutes variations in surface-exposed locations and leads to increased ATPase activity, no change in the kd value for human protein UBXD9
naturally occurring mutation, constitutes variations in surface-exposed locations and leads to increased ATPase activity and a twofold increased kd for human protein UBXD9
site-directed mutagenesis, a pore loop mutant, displays essentially unchanged oligomerization, introducing E243A point mutation increases the affinity of peptide C binding by 3fold, shows reduced ATPase activity compared to the wild-type
site-directed mutagenesis, pore loop mutant, displays essentially unchanged oligomerization, the double mutant binds peptides 4fold (peptide C) or 10fold (peptide B) more tightly than wild-type Vps4p, shows reduced ATPase activity compared to the wild-type
site-directed mutagenesis, a pore loop mutant, displays essentially unchanged oligomerization, introducing E247A point mutation increases the affinity of peptide C binding by 4fold, shows reduced ATPase activity compared to the wild-type
the Walker A mutation to the D1 domain alone shows a moderate decrease in ATPase activity, has reduced affinity for nucleotide in the D1 domain and so contains little prebound ADP
a mutant protein with very low ATPase activity. In the presence of ADP recombinant mutant enzyme forms dimers. In contrast, the addition of ATP results in the formation of a large complex with at least ten subunits