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.

Related Articles Solution NMR structure of RHE_CH02687 from Rhizobium etli: A novel flavonoid-binding protein.

Proteins. 2017 Feb 03;:

Authors: Liang C, Zhu J, Hu R, Ramelot TA, Kennedy MA, Liu M, Yang Y

Abstract
We report the solution NMR structure of RHE_CH02687 from Rhizobium etli. Its structure consists of two ?-sheets that together with two short and one long ?-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. This article is protected by copyright. All rights reserved.


PMID: 28160315 [PubMed - as supplied by publisher]



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