2F9I

Crystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureus

2F9I の概要

• エントリーDOI: 10.2210/pdb2f9i/pdb
• 関連するPDBエントリー: 2F9Y
• 分子名称: acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, ZINC ION, ... (4 entities in total)
• 機能のキーワード: zinc ribbon, crotonase superfamily, spiral domain, transferase
• 由来する生物種: Staphylococcus aureus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 137333.88

構造登録者

Bilder, P.W. (登録日: 2005-12-05, 公開日: 2006-12-05, 最終更新日: 2023-08-30)

主引用文献

Bilder, P.,Lightle, S.,Bainbridge, G.,Ohren, J.,Finzel, B.,Sun, F.,Holley, S.,Al-Kassim, L.,Spessard, C.,Melnick, M.,Newcomer, M.,Waldrop, G.L.
The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme.
Biochemistry, 45:1712-1722, 2006

PubMed Abstract: Acetyl-coA carboxylase (ACC) is a central metabolic enzyme that catalyzes the committed step in fatty acid biosynthesis: biotin-dependent conversion of acetyl-coA to malonyl-coA. The bacterial carboxyltransferase (CT) subunit of ACC is a target for the design of novel therapeutics that combat severe, hospital-acquired infections resistant to the established classes of frontline antimicrobials. Here, we present the structures of the bacterial CT subunits from two prevalent nosocomial pathogens, Staphylococcus aureus and Escherichia coli, at a resolution of 2.0 and 3.0 A, respectively. Both structures reveal a small, independent zinc-binding domain that lacks a complement in the primary sequence or structure of the eukaryotic homologue.

PubMed: 16460018
DOI: 10.1021/bi0520479

実験手法

X-RAY DIFFRACTION (1.98 Å)