Unknown

Dataset Information

0

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


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. Proteins 2017; 85:951-956. © 2016 Wiley Periodicals, Inc.

SUBMITTER: Liang C 

PROVIDER: S-EPMC5389906 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

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]

Similar Datasets

2023-11-13 | GSE228855 | GEO
| S-EPMC2533772 | biostudies-literature
| S-EPMC2855743 | biostudies-literature
| S-EPMC4959190 | biostudies-literature
| S-EPMC135151 | biostudies-literature
| S-EPMC2832352 | biostudies-literature
| S-EPMC26630 | biostudies-literature
| S-EPMC3366507 | biostudies-literature
| S-EPMC134943 | biostudies-literature
| S-EPMC27157 | biostudies-literature