来自墨西哥根瘤菌的RHE_CH02687的溶液核磁共振结构：一种新型类黄酮结合蛋白。
Solution NMR structure of RHE_CH02687 from Rhizobium etli: A novel flavonoid-binding protein.
作者信息
Liang Chunjie, Zhu Jiang, Hu Rui, Ramelot Theresa A, Kennedy Michael A, Liu Maili, Yang Yunhuang
机构信息
State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, Wuhan Center for Magnetic Resonance, CAS Key Laboratory of Magnetic Resonance in Biological Systems, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071, China.
Department of Chemistry and Biochemistry, and the Northeast Structural Genomics Consortium, Miami University, Oxford, Ohio, 45056.
出版信息
Proteins. 2017 May;85(5):951-956. doi: 10.1002/prot.25258. Epub 2017 Feb 16.
We report the solution NMR structure of RHE_CH02687 from Rhizobium etli. Its structure consists of two β-sheets that together with two short and one long α-helix form a hydrophobic cavity. This protein shows a high structural similarity to the prokaryotic protein YndB from Bacillus subtilis, and the eukaryotic protein Aha1. NMR titration experiments confirmed that RHE_CH02687, like its homolog YndB, interacted with flavonoids, giving support for a biological function as a flavonoid sensor in the symbiotic interaction between R. etli and plants. In addition, our study showed no evidence for a direct interaction between RHE_CH02687 and HtpG, the R. etli homolog of Hsp90. Proteins 2017; 85:951-956. © 2016 Wiley Periodicals, Inc.
我们报道了来自墨西哥根瘤菌（Rhizobium etli）的RHE_CH02687的溶液核磁共振结构。其结构由两个β折叠组成，这两个β折叠与两个短α螺旋和一个长α螺旋共同形成一个疏水腔。该蛋白质与来自枯草芽孢杆菌（Bacillus subtilis）的原核蛋白质YndB以及真核蛋白质Aha1具有高度的结构相似性。核磁共振滴定实验证实，RHE_CH02687与其同源物YndB一样，与黄酮类化合物相互作用，这支持了其在墨西哥根瘤菌与植物共生相互作用中作为黄酮类传感器的生物学功能。此外，我们的研究没有发现RHE_CH02687与Hsp90的墨西哥根瘤菌同源物HtpG之间存在直接相互作用的证据。《蛋白质》2017年；85：951 - 956。© 2016威利期刊公司。
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