3ONT

The Crystal Structure of Spot14, a modulator of lipogenesis

Summary for 3ONT

• Entry DOI: 10.2210/pdb3ont/pdb
• Descriptor: Spot 14 protein (2 entities in total)
• Functional Keywords: alpha-helical, helical bundle, unknown function
• Biological source: Mus musculus (mouse)
• Cellular location: Nucleus: Q62264
• Total number of polymer chains: 1
• Total formula weight: 17538.83

Authors

Colbert, C.L.,Kwon, H.J.,Deisenhofer, J. (deposition date: 2010-08-30, release date: 2011-01-19, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.65 Å)