Solution NMR structure of RHE_CH02687 from Rhizobium etli: A novel flavonoid-binding protein.
Solution NMR structure of RHE_CH02687 from Rhizobium etli: A novel flavonoid-binding protein.
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作者：
Liang C;Zhu J;Hu R;Ramelot TA;Kennedy MA;Liu M;Yang Y
我们报告了来自Rhizobium etli的RHE_CH 02687的溶液NMR结构。它的结构由两个β-折叠，与两个短的和一个长的α-螺旋一起形成疏水空腔。该蛋白质与枯草杆菌的原核蛋白YndB和真核蛋白Aha 1具有高度的结构相似性。NMR滴定实验证实，RHE_CH02687，像它的同系物YndB，与黄酮类化合物相互作用，提供支持的生物功能，作为一个黄酮类化合物传感器之间的共生相互作用R。etli和植物。此外，我们的研究表明，没有证据表明RHE_CH02687和HtpG之间的直接相互作用，R.热休克蛋白90的同源物。
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.