与ATP-柠檬酸裂解酶的ATP结合结构域结合的ADP-Mg2+。
ADP-Mg2+ bound to the ATP-grasp domain of ATP-citrate lyase.
作者信息
Sun Tianjun, Hayakawa Koto, Fraser Marie E
机构信息
Department of Biological Sciences, University of Calgary, 2500 University Drive NW, Calgary, AB T2N 1N4, Canada.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1168-72. doi: 10.1107/S1744309111028363. Epub 2011 Sep 24.
Abstract
Human ATP-citrate lyase (EC 2.3.3.8) is the cytoplasmic enzyme that catalyzes the production of acetyl-CoA from citrate, CoA and ATP. The amino-terminal portion of the enzyme, containing residues 1-817, was crystallized in the presence of tartrate, ATP and magnesium ions. The crystals diffracted to 2.3 Å resolution. The structure shows ADP-Mg(2+) bound to the domain that possesses the ATP-grasp fold. The structure demonstrates that this crystal form could be used to investigate the structures of complexes with inhibitors of ATP-citrate lyase that bind at either the citrate- or ATP-binding site.
摘要
人ATP-柠檬酸裂解酶（EC 2.3.3.8）是一种细胞质酶，可催化由柠檬酸、辅酶A和ATP生成乙酰辅酶A。该酶的氨基末端部分（包含第1至817位残基）在酒石酸盐、ATP和镁离子存在的情况下结晶。晶体衍射分辨率达到2.3 Å。结构显示ADP-Mg(2+)与具有ATP结合折叠结构域结合。该结构表明，这种晶体形式可用于研究与在柠檬酸或ATP结合位点结合的ATP-柠檬酸裂解酶抑制剂形成的复合物的结构。
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