Solution Structures of Spinach Acyl Carrier Protein with Decanoate and Stearate

详细信息    查看全文

• 作者：Gregory A. Zornetzer ; Brian G. Fox ; and John L. Markley
• 刊名：Biochemistry
• 出版年：2006
• 出版时间：April 25, 2006
• 年：2006
• 卷：45
• 期：16
• 页码：5217 - 5227
• 全文大小：792K
• 年卷期：v.45,no.16(April 25, 2006)
• ISSN：1520-4995

文摘

Acyl carrier protein (ACP) is a cofactor in a variety of biosynthetic pathways, including fattyacid metabolism. Thus, it is of interest to determine structures of physiologically relevant ACP-fattyacid complexes. We report here the NMR solution structures of spinach ACP with decanoate (10:0-ACP)and stearate (18:0-ACP) attached to the 4'-phosphopantetheine prosthetic group. The protein in the fattyacid complexes adopts a single conformer, unlike apo- and holo-ACP, which interconvert in solutionbetween two major conformers. The protein component of both 10:0- and 18:0-ACP adopts the four-helix bundle topology characteristic of ACP, and a fatty acid binding cavity was identified in both structures.Portions of the protein close in space to the fatty acid and the 4'-phosphopantetheine were identifiedusing filtered/edited NOESY experiments. A docking protocol was used to generate protein structurescontaining bound fatty acid for 10:0- and 18:0-ACP. In both cases, the predominant structure containedfatty acid bound down the center of the helical bundle, in agreement with the location of the fatty acidbinding pockets. These structures demonstrate the conformational flexibility of spinach ACP and suggesthow the protein changes to accommodate its myriad binding partners.