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Solution NMR structure of RHE_CH02687 from Rhizobium etli : A novel flavonoid‐binding protein
Author(s) -
Liang Chunjie,
Zhu Jiang,
Hu Rui,
Ramelot Theresa A.,
Kennedy Michael A.,
Liu Maili,
Yang Yunhuang
Publication year - 2017
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25258
Subject(s) - bacillus subtilis , two dimensional nuclear magnetic resonance spectroscopy , rhizobium , biochemistry , structural similarity , chemistry , biology , crystallography , stereochemistry , bacteria , gene , genetics
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. © 2016 Wiley Periodicals, Inc.