铜绿假单胞菌全酰基载体蛋白的¹H、¹³C和¹⁵N归属
¹H, ¹³C and ¹⁵N assignments of the holo-acyl carrier protein of Pseudomonas aeruginosa.
作者信息
Duggan Brendan M, Roca Amancio, Zhang Yong-Mei
机构信息
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, 173 Ashley Ave., Charleston, SC 29425, USA.
出版信息
Biomol NMR Assign. 2013 Oct;7(2):225-8. doi: 10.1007/s12104-012-9415-9. Epub 2012 Jul 29.
Abstract
Acyl carrier proteins (ACPs) are a group of highly conserved and abundant proteins in bacteria. ACPs play a central role as the acyl group carriers in bacterial fatty acid biosynthesis, providing building blocks for membrane biogenesis and the production of secondary metabolites. In the versatile human pathogen Pseudomonas aeruginosa, three ACP homologs have been identified. One homolog, AcpP, exhibits the strongest sequence homology to the canonical Escherichia coli ACP. Here we report the (1)H, (13)C and (15)N assignments of the holo-AcpP of P. aeruginosa.
摘要
酰基载体蛋白（ACPs）是细菌中一组高度保守且含量丰富的蛋白质。ACPs作为细菌脂肪酸生物合成中的酰基载体发挥核心作用，为膜生物发生和次生代谢产物的产生提供构建模块。在多能人类病原体铜绿假单胞菌中，已鉴定出三种ACPs同源物。其中一种同源物AcpP与典型的大肠杆菌ACP具有最强的序列同源性。在此，我们报告了铜绿假单胞菌全酶形式的AcpP的氢-1、碳-13和氮-15化学位移归属。
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