Solution NMR structure of RHE_CH02687 from Rhizobium etli: A novel flavonoid-binding protein.
Proteins
; 85(5): 951-956, 2017 05.
Article
em En
| MEDLINE
| ID: mdl-28160315
ABSTRACT
We report the solution NMR structure of RHE_CH02687 from Rhizobium etli. Its structure consists of two ß-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; 85951-956. © 2016 Wiley Periodicals, Inc.
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Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Flavonoides
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Rhizobium etli
Idioma:
En
Revista:
Proteins
Assunto da revista:
BIOQUIMICA
Ano de publicação:
2017
Tipo de documento:
Article
País de afiliação:
China