5AB7
Crystal structure of Trypanosoma brucei SCP2-thiolase like protein (TbSLP) in complex with malonyl-CoA.
5AB7 の概要
| エントリーDOI | 10.2210/pdb5ab7/pdb |
| 関連するPDBエントリー | 5AB4 5AB5 5AB6 |
| 分子名称 | SCP2-THIOLASE LIKE PROTEIN, MALONYL-COENZYME A, SULFATE ION, ... (4 entities in total) |
| 機能のキーワード | transport protein, coenzyme a, scp2-thiolase, scp2-thiolase- like protein, malonyl-coa decarboxylase, gene knockout, lipid metabolism |
| 由来する生物種 | TRYPANOSOMA BRUCEI BRUCEI |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 278661.75 |
| 構造登録者 | |
| 主引用文献 | Harijan, R.K.,Mazet, M.,Kiema, T.R.,Bouyssou, G.,Alexson, S.E.H.,Bergmann, U.,Moreau, P.,Michels, P.A.M.,Bringaud, F.,Wierenga, R.K. The Scp2-Thiolase-Like Protein (Slp) of Trypanosoma Brucei is an Enzyme Involved in Lipid Metabolism. Proteins, 84:1075-, 2016 Cited by PubMed Abstract: Bioinformatics studies have shown that the genomes of trypanosomatid species each encode one SCP2-thiolase-like protein (SLP), which is characterized by having the YDCF thiolase sequence fingerprint of the Cβ2-Cα2 loop. SLPs are only encoded by the genomes of these parasitic protists and not by those of mammals, including human. Deletion of the Trypanosoma brucei SLP gene (TbSLP) increases the doubling time of procyclic T. brucei and causes a 5-fold reduction of de novo sterol biosynthesis from glucose- and acetate-derived acetyl-CoA. Fluorescence analyses of EGFP-tagged TbSLP expressed in the parasite located the TbSLP in the mitochondrion. The crystal structure of TbSLP (refined at 1.75 Å resolution) confirms that TbSLP has the canonical dimeric thiolase fold. In addition, the structures of the TbSLP-acetoacetyl-CoA (1.90 Å) and TbSLP-malonyl-CoA (2.30 Å) complexes reveal that the two oxyanion holes of the thiolase active site are preserved. TbSLP binds malonyl-CoA tightly (Kd 90 µM), acetoacetyl-CoA moderately (Kd 0.9 mM) and acetyl-CoA and CoA very weakly. TbSLP possesses low malonyl-CoA decarboxylase activity. Altogether, the data show that TbSLP is a mitochondrial enzyme involved in lipid metabolism. Proteins 2016; 84:1075-1096. © 2016 Wiley Periodicals, Inc. PubMed: 27093562DOI: 10.1002/PROT.25054 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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