3K6M

Dynamic domains of Succinyl-CoA:3-ketoacid-coenzyme A transferase from pig heart.

3K6M の概要

• エントリーDOI: 10.2210/pdb3k6m/pdb
• 関連するPDBエントリー: 1M3E 1O9L 1OOY 1OOZ 1OPE 2NRB
• 分子名称: Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial, CHLORIDE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: scot, coa transferase, dynamic domain, glycerol, mitochondrion, transferase, transit peptide
• 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: 4
• 化学式量合計: 209430.92

構造登録者

Coker, S.,Lloyd, A.,Mitchell, E.,Lewis, G.R.,Shoolingin-Jordan, P.,Coker, A.R. (登録日: 2009-10-09, 公開日: 2010-07-07, 最終更新日: 2023-09-06)

主引用文献

Coker, S.F.,Lloyd, A.J.,Mitchell, E.,Lewis, G.R.,Coker, A.R.,Shoolingin-Jordan, P.M.
The high-resolution structure of pig heart succinyl-CoA:3-oxoacid coenzyme A transferase.
Acta Crystallogr.,Sect.D, 66:797-805, 2010

PubMed Abstract: The enzyme succinyl-CoA:3-oxoacid coenzyme A transferase (SCOT) participates in the metabolism of ketone bodies in extrahepatic tissues. It catalyses the transfer of coenzyme A (CoA) from succinyl-CoA to acetoacetate with a classical ping-pong mechanism. There is biochemical evidence that the enzyme undergoes conformational changes during the reaction, but no domain movements have been reported in the available crystal structures. Here, a structure of pig heart SCOT refined at 1.5 A resolution is presented, showing that one of the four enzyme subunits in the crystallographic asymmetric unit has a molecule of glycerol bound in the active site; the glycerol molecule is hydrogen bonded to the conserved catalytic glutamate residue and is likely to occupy the cosubstrate-binding site. The binding of glycerol is associated with a substantial relative movement (a 13 degrees rotation) of two previously undefined domains that close around the substrate-binding site. The binding orientation of one of the cosubstrates, acetoacetate, is suggested based on the glycerol binding and the possibility that this dynamic domain movement is of functional importance is discussed.

PubMed: 20606260
DOI: 10.1107/S0907444910018366

実験手法

X-RAY DIFFRACTION (1.5 Å)