Premium
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom