4F0X

Crystal structure of human Malonyl-CoA Decarboxylase (Peroxisomal Isoform)

4F0X の概要

• エントリーDOI: 10.2210/pdb4f0x/pdb
• 分子名称: Malonyl-CoA decarboxylase, mitochondrial, N~3~-[(2R)-2-hydroxy-4-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}-3,3-dimethylbutanoyl]-beta-alaninamide (2 entities in total)
• 機能のキーワード: enzyme, peroxisome, lyase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion: O95822
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 411766.31

構造登録者

Aparicio, D.,Perez, R.,Fita, I. (登録日: 2012-05-05, 公開日: 2013-03-20, 最終更新日: 2024-02-28)

主引用文献

Aparicio, D.,Perez-Luque, R.,Carpena, X.,Diaz, M.,Ferrer, J.C.,Loewen, P.C.,Fita, I.
Structural Asymmetry and Disulfide Bridges among Subunits Modulate the Activity of Human Malonyl-CoA Decarboxylase.
J.Biol.Chem., 288:11907-11919, 2013

PubMed Abstract: Decarboxylation of malonyl-CoA to acetyl-CoA by malonyl-CoA decarboxylase (MCD; EC 4.1.1.9) is an essential facet in the regulation of fatty acid metabolism. The structure of human peroxisomal MCD reveals a molecular tetramer that is best described as a dimer of structural heterodimers, in which the two subunits present markedly different conformations. This molecular organization is consistent with half-of-the-sites reactivity. Each subunit has an all-helix N-terminal domain and a catalytic C-terminal domain with an acetyltransferase fold (GNAT superfamily). Intersubunit disulfide bridges, Cys-206-Cys-206 and Cys-243-Cys-243, can link the four subunits of the tetramer, imparting positive cooperativity to the catalytic process. The combination of a half-of-the-sites mechanism within each structural heterodimer and positive cooperativity in the tetramer produces a complex regulatory picture that is further complicated by the multiple intracellular locations of the enzyme. Transport into the peroxisome has been investigated by docking human MCD onto the peroxisomal import protein peroxin 5, which revealed interactions that extend beyond the C-terminal targeting motif.

PubMed: 23482565
DOI: 10.1074/jbc.M112.443846

実験手法

X-RAY DIFFRACTION (3.29 Å)