[HTML][HTML] Active glutaminase C self-assembles into a supratetrameric oligomer that can be disrupted by an allosteric inhibitor
APS Ferreira, A Cassago… - Journal of Biological …, 2013 - ASBMB
The phosphate-dependent transition between enzymatically inert dimers into catalytically
capable tetramers has long been the accepted mechanism for the glutaminase activation.
Here, we demonstrate that activated glutaminase C (GAC) self-assembles into a helical,
fiber-like double-stranded oligomer and propose a molecular model consisting of seven
tetramer copies per turn per strand interacting via the N-terminal domains. The loop 321
LRFNKL 326 is projected as the major regulating element for self-assembly and enzyme …
capable tetramers has long been the accepted mechanism for the glutaminase activation.
Here, we demonstrate that activated glutaminase C (GAC) self-assembles into a helical,
fiber-like double-stranded oligomer and propose a molecular model consisting of seven
tetramer copies per turn per strand interacting via the N-terminal domains. The loop 321
LRFNKL 326 is projected as the major regulating element for self-assembly and enzyme …