Solution structure and function of YndB, an AHSA1 protein from Bacillus subtilis

Jaime L. Stark, Kelly A. Mercier, Geoffrey A. Mueller, Thomas B. Acton, Rong Xiao, Gaetano T. Montelione, Robert Powers

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The solution structure of the Bacillus subtilis protein YndB has been solved using NMR 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 with 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. On the basis of these similarities, YndB has been classified as a member of the activator of Hsp90 ATPase homolog 1-like 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 thesymbiotic relationship between B. subtilis and plants. Proteins 2010.

Original languageEnglish (US)
Pages (from-to)3328-3340
Number of pages13
JournalProteins: Structure, Function and Bioinformatics
Volume78
Issue number16
DOIs
StatePublished - Dec 1 2010

Fingerprint

Activator Appliances
Chalcone
Bacilli
Bacillus subtilis
flavone
Adenosine Triphosphatases
Lipids
Proteins
Eukaryota
Flavonoids
Computer Simulation
Molecules
Nuclear magnetic resonance
Archaea
Hand Strength
Pathogens
Titration
Anti-Bacterial Agents
Infection
Experiments

Keywords

  • Chalcones
  • In silico screen
  • NMR ligand affinity screen
  • NMR structure
  • Stress response
  • Symbiotic relationship
  • YndB Bacillus subtilis

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Cite this

Stark, J. L., Mercier, K. A., Mueller, G. A., Acton, T. B., Xiao, R., Montelione, G. T., & Powers, R. (2010). Solution structure and function of YndB, an AHSA1 protein from Bacillus subtilis. Proteins: Structure, Function and Bioinformatics, 78(16), 3328-3340. https://doi.org/10.1002/prot.22840

Solution structure and function of YndB, an AHSA1 protein from Bacillus subtilis. / Stark, Jaime L.; Mercier, Kelly A.; Mueller, Geoffrey A.; Acton, Thomas B.; Xiao, Rong; Montelione, Gaetano T.; Powers, Robert.

In: Proteins: Structure, Function and Bioinformatics, Vol. 78, No. 16, 01.12.2010, p. 3328-3340.

Research output: Contribution to journalArticle

Stark, JL, Mercier, KA, Mueller, GA, Acton, TB, Xiao, R, Montelione, GT & Powers, R 2010, 'Solution structure and function of YndB, an AHSA1 protein from Bacillus subtilis', Proteins: Structure, Function and Bioinformatics, vol. 78, no. 16, pp. 3328-3340. https://doi.org/10.1002/prot.22840
Stark, Jaime L. ; Mercier, Kelly A. ; Mueller, Geoffrey A. ; Acton, Thomas B. ; Xiao, Rong ; Montelione, Gaetano T. ; Powers, Robert. / Solution structure and function of YndB, an AHSA1 protein from Bacillus subtilis. In: Proteins: Structure, Function and Bioinformatics. 2010 ; Vol. 78, No. 16. pp. 3328-3340.
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