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Function
ATP-citrate synthase (ACS) is part of the citrate cycle. It catalyzes the transformation of ADP, acetyl-CoA and oxaloacetate to ATP, citrate and CoA. ACS is the link between energy metabolism from carbohydrates to the production of fatty acids.
See also Citrate Synthase
Structural highlights
Crystal structures have shown that tartrate and citrate bind to ACS in the same binding site. Binding site of tartrate of ATP-citrate synthase. Binding site of ADP and Mg+2 ions , 3pff. [1]
- ↑ Sun T, Hayakawa K, Fraser ME. ADP-Mg2+ bound to the ATP-grasp domain of ATP-citrate lyase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1168-72., Epub 2011 Sep 24. PMID:22102020 doi:10.1107/S1744309111028363
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3D Structures of ATP-citrate synthase
Updated on 22-March-2018
Citrate Synthase, 3pff – hACS + citrate – human
5tdf, 5tet – hACS + citrate derivative
5teq – hACS N-terminal (mutant) + citrate
5te1 – hACS N-terminal (mutant) + citrate derivative
5tes – hACS + citrate + ADP
5tdm – hACS + citrate derivative + ADP
3mwe – hACS + tartrate
3pff, 5tdz - hACS + tartrate + ADP
References
proteopedia link