1OOY

SUCCINYL-COA:3-KETOACID COA TRANSFERASE FROM PIG HEART

1OOY の概要

• エントリーDOI: 10.2210/pdb1ooy/pdb
• 関連するPDBエントリー: 1M3E
• 分子名称: Succinyl-CoA:3-ketoacid-coenzyme A transferase, mitochondrial precursor, POTASSIUM ION, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: alpha/beta protein, transferase
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Mitochondrion: Q29551
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 104839.28

構造登録者

Coros, A.M.,Swenson, L.,Wolodko, W.T.,Fraser, M.E. (登録日: 2003-03-04, 公開日: 2004-04-27, 最終更新日: 2023-08-16)

主引用文献

Coros, A.M.,Swenson, L.,Wolodko, W.T.,Fraser, M.E.
Structure of the CoA transferase from pig heart to 1.7 A resolution.
Acta Crystallogr.,Sect.D, 60:1717-1725, 2004

PubMed Abstract: Succinyl-CoA:3-ketoacid CoA transferase (SCOT; EC 2.8.3.5) activates the acetoacetate in ketone bodies by transferring the CoA group from succinyl-CoA to acetoacetate to produce acetoacetyl-CoA and succinate. In the reaction, a glutamate residue at the active site of the enzyme forms a thioester bond with CoA and in this form the enzyme is subject to autolytic fragmentation. The crystal structure of pig heart SCOT has been solved and refined to 1.7 A resolution in a new crystal form. The structure shows the active-site glutamate residue in a conformation poised for autolytic fragmentation, with its side chain accepting one hydrogen bond from Asn281 and another from its own amide N atom. However, the conformation of this glutamate side chain would have to change for the residues that are conserved in the CoA transferases (Gln99, Gly386 and Ala387) to participate in stabilizing the tetrahedral transition states of the catalytic mechanism. The structures of a deletion mutant in two different crystal forms were also solved.

PubMed: 15388917
DOI: 10.1107/S0907444904017974

実験手法

X-RAY DIFFRACTION (1.7 Å)