ATP-citrate synthase

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.

Structural highlights

Crystal structures have shown that tartrate and citrate bind to ACS in the same binding site. of ATP-citrate synthase with ADP (stick model), tartrate and Mg+2 ions (green), 3pff. ^[1]

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

Drag the structure with the mouse to rotate

3D Structures of ATP-citrate synthase3D Structures of ATP-citrate synthase

Updated on 15-November-2015

3mwd – hACS + citrate – human
3mwe – hACS + tartrate
3pff - hACS + tartrate + ADP

ReferencesReferences

↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

[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

[1]