5MGB

Crystal Structure of Rat Peroxisomal Multifunctional enzyme Type-1 (RPMFE1) Complexed with Acetoacetyl-CoA and NAD

「5AAK」から置き換えられました

5MGB の概要

• エントリーDOI: 10.2210/pdb5mgb/pdb
• 分子名称: Peroxisomal bifunctional enzyme, SULFATE ION, ACETOACETYL-COENZYME A, ... (6 entities in total)
• 機能のキーワード: oxidoreductase, acetoacetyl-coa, nad+, mfe1, beta-oxidation, fatty acid, crotonase, 3-hydroxyacyl-coa-dehydrogenase
• 由来する生物種: Rattus norvegicus (Rat)
• 細胞内の位置: Peroxisome: P07896
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 165461.21

構造登録者

Kasaragod, P.,Kiema, T.-R.,Schmitz, W.,Hiltunen, J.K.,Wierenga, R.K. (登録日: 2016-11-21, 公開日: 2016-12-21, 最終更新日: 2024-01-17)

主引用文献

Kasaragod, P.,Midekessa, G.B.,Sridhar, S.,Schmitz, W.,Kiema, T.R.,Hiltunen, J.K.,Wierenga, R.K.
Structural enzymology comparisons of multifunctional enzyme, type-1 (MFE1): the flexibility of its dehydrogenase part.
FEBS Open Bio, 7:1830-1842, 2017

PubMed Abstract: Multifunctional enzyme, type-1 (MFE1) is a monomeric enzyme with a 2E-enoyl-CoA hydratase and a 3S-hydroxyacyl-CoA dehydrogenase (HAD) active site. Enzyme kinetic data of rat peroxisomal MFE1 show that the catalytic efficiencies for converting the short-chain substrate 2E-butenoyl-CoA into acetoacetyl-CoA are much lower when compared with those of the homologous monofunctional enzymes. The mode of binding of acetoacetyl-CoA (to the hydratase active site) and the very similar mode of binding of NAD and NADH (to the HAD part) are described and compared with those of their monofunctional counterparts. Structural comparisons suggest that the conformational flexibility of the HAD and hydratase parts of MFE1 are correlated. The possible importance of the conformational flexibility of MFE1 for its biocatalytic properties is discussed.

PubMed: 29226071
DOI: 10.1002/2211-5463.12337

実験手法

X-RAY DIFFRACTION (2.8 Å)