Ontology highlight
ABSTRACT:
SUBMITTER: Liang C
PROVIDER: S-EPMC5389906 | biostudies-literature | 2017 May
REPOSITORIES: biostudies-literature
Liang Chunjie C Zhu Jiang J Hu Rui R Ramelot Theresa A TA Kennedy Michael A MA Liu Maili M Yang Yunhuang Y
Proteins 20170216 5
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 ...[more]