| Literature DB >> 28160315 |
Chunjie Liang1, Jiang Zhu1, Rui Hu1, Theresa A Ramelot2, Michael A Kennedy2, Maili Liu1, Yunhuang Yang1.
Abstract
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.Entities:
Keywords: AHSA1 family; NMR titration; flavonoid binding; hydrophobic cavity; symbiotic
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Year: 2017 PMID: 28160315 PMCID: PMC5389906 DOI: 10.1002/prot.25258
Source DB: PubMed Journal: Proteins ISSN: 0887-3585