3ONT

The Crystal Structure of Spot14, a modulator of lipogenesis

3ONT の概要

• エントリーDOI: 10.2210/pdb3ont/pdb
• 分子名称: Spot 14 protein (2 entities in total)
• 機能のキーワード: alpha-helical, helical bundle, unknown function
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Nucleus: Q62264
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17538.83

構造登録者

Colbert, C.L.,Kwon, H.J.,Deisenhofer, J. (登録日: 2010-08-30, 公開日: 2011-01-19, 最終更新日: 2024-10-30)

主引用文献

Colbert, C.L.,Kim, C.W.,Moon, Y.A.,Henry, L.,Palnitkar, M.,McKean, W.B.,Fitzgerald, K.,Deisenhofer, J.,Horton, J.D.,Kwon, H.J.
Crystal structure of Spot 14, a modulator of fatty acid synthesis.
Proc.Natl.Acad.Sci.USA, 107:18820-18825, 2010

PubMed Abstract: Spot 14 (S14) is a protein that is abundantly expressed in lipogenic tissues and is regulated in a manner similar to other enzymes involved in fatty acid synthesis. Deletion of S14 in mice decreased lipid synthesis in lactating mammary tissue, but the mechanism of S14's action is unknown. Here we present the crystal structure of S14 to 2.65 Å and biochemical data showing that S14 can form heterodimers with MIG12. MIG12 modulates fatty acid synthesis by inducing the polymerization and activity of acetyl-CoA carboxylase, the first committed enzymatic reaction in the fatty acid synthesis pathway. Coexpression of S14 and MIG12 leads to heterodimers and reduced acetyl-CoA carboxylase polymerization and activity. The structure of S14 suggests a mechanism whereby heterodimer formation with MIG12 attenuates the ability of MIG12 to activate ACC.

PubMed: 20952656
DOI: 10.1073/pnas.1012736107

実験手法

X-RAY DIFFRACTION (2.65 Å)