6NZY

Structural Determination of the Carboxy-terminal portion of ATP-citrate lyase

6NZY の概要

• エントリーDOI: 10.2210/pdb6nzy/pdb
• 分子名称: ATP-citrate lyase alpha-subunit, ACETYL COENZYME *A, PHOSPHATE ION, ... (6 entities in total)
• 機能のキーワード: carboxy-terminal portion, acetyl-coa, acyl-coa synthetase, lyase
• 由来する生物種: Chlorobium limicola
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 118877.30

構造登録者

Nguyen, V.H.,Fraser, M.E. (登録日: 2019-02-14, 公開日: 2019-12-18, 最終更新日: 2023-10-11)

主引用文献

Nguyen, V.H.,Singh, N.,Medina, A.,Uson, I.,Fraser, M.E.
Identification of the active site residues in ATP-citrate lyase's carboxy-terminal portion.
Protein Sci., 28:1840-1849, 2019

PubMed Abstract: ATP-citrate lyase (ACLY) catalyzes production of acetyl-CoA and oxaloacetate from CoA and citrate using ATP. In humans, this cytoplasmic enzyme connects energy metabolism from carbohydrates to the production of lipids. In certain bacteria, ACLY is used to fix carbon in the reductive tricarboxylic acid cycle. The carboxy(C)-terminal portion of ACLY shows sequence similarity to citrate synthase of the tricarboxylic acid cycle. To investigate the roles of residues of ACLY equivalent to active site residues of citrate synthase, these residues in ACLY from Chlorobium limicola were mutated, and the proteins were investigated using kinetics assays and biophysical techniques. To obtain the crystal structure of the C-terminal portion of ACLY, full-length C. limicola ACLY was cleaved, first non-specifically with chymotrypsin and subsequently with Tobacco Etch Virus protease. Crystals of the C-terminal portion diffracted to high resolution, providing structures that show the positions of active site residues and how ACLY tetramerizes.

PubMed: 31411782
DOI: 10.1002/pro.3708

実験手法

X-RAY DIFFRACTION (1.9 Å)