Department of Chemistry
Date of this Version
2010
Citation
Proteins. 2010 December ; 78(16): 3328–3340. doi:10.1002/prot.22840.
Abstract
The solution structure of the Bacillus subtilis protein YndB has been solved using NMR in order to investigate proposed biological functions. The YndB structure exhibits the helix-grip fold, which consists of a β-sheet with two small and one long α-helix, forming a hydrophobic cavity that preferentially binds lipid-like molecules. Sequence and structure comparisons to proteins from eukaryotes, prokaryotes, and archaea suggest that YndB is very similar to the eukaryote protein Aha1, which binds to the middle domain of Hsp90 and induces ATPase activity. Based on these similarities, YndB has been classified as a member of the Activator of Hsp90 ATPase homologlike protein (AHSA1) family with a function that appears to be related to stress response. An in silico screen of a compound library of ~18,500 lipids was used to identify classes of lipids that preferentially bind YndB. The in silico screen identified, in order of affinity, the chalcone/ hydroxychalcone, flavanone, and flavone/flavonol classes of lipids, which was further verified by 2D 1H-15N HSQC NMR titration experiments with trans-chalcone, flavanone, flavone, and flavonol. All of these compounds are typically found in plants as precursors to various flavonoid antibiotics and signaling molecules. The sum of the data suggests an involvement of YndB with the stress response of B. subtilis to chalcone-like flavonoids released by plants due to a pathogen infection. The observed binding of chalcone-like molecules by YndB is likely related to the symbiotic relationship between B. subtilis and plants.
Comments
Copyright 2010 Wiley-Liss, Inc.