@article {48104,
	title = {A near-atomic structure of the dark apoptosome provides insight into assembly and activation.},
	journal = {Structure (London, England : 1993)},
	volume = {25},
	year = {2016},
	month = {2016 Nov 16},
	pages = {40-52},
	abstract = {<p>In Drosophila, the Apaf-1-related killer (Dark) forms an apoptosome that activates procaspases. To investigate function, we have determined a near-atomic structure of Dark double rings using cryo-electron microscopy. We then built a nearly complete model of the apoptosome that includes 7- and 8-blade β-propellers. We find that the preference for dATP during Dark assembly may be governed by Ser325, which is in close proximity to the 2{\textquoteright} carbon of the deoxyribose ring. Interestingly, β-propellers in V-shaped domains of the Dark apoptosome are more widely separated, relative to these features in the Apaf-1 apoptosome. This wider spacing may be responsible for the lack of cytochrome c binding to β-propellers in the Dark apoptosome. Our structure also highlights the roles of two loss-of-function mutations that may block Dark assembly. Finally, the improved model provides a framework to understand apical procaspase activation in the intrinsic cell death pathway.</p>
},
	issn = {1878-4186},
	doi = {10.1016/j.str.2016.11.002},
	author = {Cheng, Tat Cheung and Akey, Ildik{\'o} V and Yuan, Shujun and Yu, Zhiheng and Ludtke, Steven J and Akey, Christopher W}
}
