ATP-citrate synthase

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spinqualitylabelsall models ATP-citrate synthase complex with ADP (stick model), tartrate and Mg+2 ions (green), 3pff Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image 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. of ATP-citrate synthase. Water molecules are shown as red spheres. , 3pff. [1]

3D Structures of ATP-citrate synthase

Updated on 14-May-2018

3mwd, 5tde – 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

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