1OD2

Acetyl-CoA Carboxylase Carboxyltransferase Domain

1OD2 の概要

• エントリーDOI: 10.2210/pdb1od2/pdb
• 関連するPDBエントリー: 1OD4
• 分子名称: ACETYL-COENZYME A CARBOXYLASE, ACETYL COENZYME *A, ADENINE, ... (4 entities in total)
• 機能のキーワード: ligase, acc, acetyl-coa, acetyl-coa carboxylase, obesity
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 184931.54

構造登録者

Zhang, H.,Yang, Z.,Shen, Y.,Tong, L. (登録日: 2003-02-12, 公開日: 2003-04-03, 最終更新日: 2024-10-16)

主引用文献

Zhang, H.,Yang, Z.,Shen, Y.,Tong, L.
Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase.
Science, 299:2064-2067, 2003

PubMed Abstract: Acetyl-coenzyme A carboxylases (ACCs) are required for the biosynthesis and oxidation of long-chain fatty acids. They are targets for therapeutics against obesity and diabetes, and several herbicides function by inhibiting their carboxyltransferase (CT) domain. We determined the crystal structure of the free enzyme and the coenzyme A complex of yeast CT at 2.7 angstrom resolution and found that it comprises two domains, both belonging to the crotonase/ClpP superfamily. The active site is at the interface of a dimer. Mutagenesis and kinetic studies reveal the functional roles of conserved residues here. The herbicides target the active site of CT, providing a lead for inhibitor development against human ACCs.

PubMed: 12663926
DOI: 10.1126/science.1081366

実験手法

X-RAY DIFFRACTION (2.7 Å)