The Structure of the Carboxyltransferase Component of Acetyl-CoA Carboxylase Reveals a Zinc-Binding Motif Unique to the Bacterial Enzyme

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• 作者：Patrick Bilder ; Sandra Lightle ; Graeme Bainbridge ; Jeffrey Ohren ; Barry Finzel ; Fang Sun ; Susan Holley ; Loola Al-Kassim ; Cindy Spessard ; Michael Melnick ; Marcia Newcomer ; and Grover L. Waldrop
• 刊名：Biochemistry
• 出版年：2006
• 出版时间：February 14, 2006
• 年：2006
• 卷：45
• 期：6
• 页码：1712 - 1722
• 全文大小：1655K
• 年卷期：v.45,no.6(February 14, 2006)
• ISSN：1520-4995

文摘

Acetyl-coA carboxylase (ACC) is a central metabolic enzyme that catalyzes the committedstep in fatty acid biosynthesis: biotin-dependent conversion of acetyl-coA to malonyl-coA. The bacterialcarboxyltransferase (CT) subunit of ACC is a target for the design of novel therapeutics that combatsevere, 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 Å, respectively. Both structuresreveal a small, independent zinc-binding domain that lacks a complement in the primary sequence orstructure of the eukaryotic homologue.