IndraLab

Statements



sparser
"Previous study suggested that subunit H inhibits the ATPase activity of the dissociated V1 domain, thereby preventing its nonproductive ATP hydrolysis ( Beyenbach & Wieczorek, 2006 )."

sparser
"This structure appears to be an inhibitory state wherein the subunit H inhibits the ATPase activity by stabilizing ADP binding to the catalytic site."

sparser
"Together with biochemical data, the structure supports a mechanistic model wherein subunit H inhibits ATPase activity by stabilizing an open catalytic site that results in tight binding of inhibitory ADP at another site."

sparser
"Previous structural studies of V 1 subcomplexes showed that while subunit H inhibited V 1 -ATPase is mostly in state 2 (Oot et al, xref ; Vasanthakumar et al, xref ), Oxr1p-bound V 1 is found exclusively in state 1 (Khan et al, xref )."