ATP-citrate synthase

From Proteopedia

Function

ATP-citrate synthase (ACS) or ATP citrate lyase or citryl-CoA synthetase 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.

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. Water molecules are shown as red spheres. Binding site of ADP and Mg+2 ions, 3pff. ^[1]

3D Structures of ATP-citrate synthase

ATP-citrate synthase 3D structures

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ATP-citrate synthase complex with ADP (stick model), tartrate and Mg+2 ions (green), 3pff

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References

↑ 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