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Human START domain of Acyl-coenzyme A thioesterase 11

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PDB Code 3FO5 Target Class Lipid signalling Target ACOT11 Alias ACOT11, BFIT, BFIT1, BFIT2, KIAA0707, STARD14, THEA, THEM1 Disease Area/Function Date Deposited Dec 27 2008 Authors Siponen, M.I., Lehtio, L., Moche, M., Arrowsmith, C.H., Berglund, H., Bountra, C., Collins, R., Dahlgren, L.G., Edwards, A.M., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Johansson, A., Johansson, I., Karlberg, T., Kotenyova, T., Nilsson, M.E., Nordlund, P, Nyman, T., Persson, C., Sagemark, J., Thorsell, A.G., Tresaugues, L., Van Den Berg, S., Weigelt, J., Welin, M., Wikstrom, M., Wisniewska, M., Schueler, H.

About this structure

Human Acyl-coenzyme A thioesterase 11, also known as brown fat-inducible thioesterase (BFIT) or STARD14, exists as two tissue-specific splice variants that differ slightly in their C-termini (1). ACOT11 expression is cold-induced, and expression levels are linked to obesity, with obesity resistant mice displaying higher ACOT11 expression than obesity-prone mice (2). The rat ortholog has acyl-CoA thioesterase activity with specificity towards medium to long-chain (C12-18) fatty acyl-CoA substrates (3).

ACOT11 consists of two thioesterase domains and a C-terminal lipid binding START (StAR-related lipid-transfer) domain. START domains are found in proteins involved in lipid metabolism, lipid trafficking and cell signaling (4). We solved the structure of the C-terminal START domain (residues 350-594) at a resolution of 2.0 Å. The structure shows a globular domain consisting of a 9-stranded antiparallel β-sheet surrounded by α-helices. The curved β-sheet, together with 4 helices on its concave side, forms a hydrophobic cavity which is the putative lipid binding site.

References

  1. Adams, S. H.; Chui, C.; Schilbach, S. L.; Yu, X. X.; Goddard, A. D.; Grimaldi, J. C.; Lee, J.; Dowd, P.; Colman, S.; Lewin, D. A. (2001) BFIT, a unique acyl-CoA thioesterase induced in thermogenic brown adipose tissue: cloning, organization of the human gene and assessment of a potential link to obesity. Biochem. J. 360: 135-142.
  2. Ishikawa, K.; Nagase, T.; Suyama, M.; Miyajima, N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O. (1998) Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 5: 169-176.
  3. Suematsu N, Okamoto K, Shibata K, Nakanishi Y, Isohashi and F. (2001) Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase. Eur. J. Biochem. 268:2700-2709.
  4. Ponting CP, Aravind L. (1999) START: a lipid-binding domain in StAR, HD-ZIP and signalling proteins. Trends Biochem. Sci. 24:130-132.