Solution structure of the PAS domain of a thermophilic YybT protein homolog reveals a potential ligand-binding site

Tan, Edward, Rao, Feng, Pasunooti, Swathi, Thi Huong Pham, Soehano, Ishin, Turner, Mark S., Liew, Chong Wai, Lescar, Julien, Pervushin, Konstantin and Liang, Zhao-Xun (2013) Solution structure of the PAS domain of a thermophilic YybT protein homolog reveals a potential ligand-binding site. Journal of Biological Chemistry, 288 17: 11949-11959. doi:10.1074/jbc.M112.437764

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Author Tan, Edward
Rao, Feng
Pasunooti, Swathi
Thi Huong Pham
Soehano, Ishin
Turner, Mark S.
Liew, Chong Wai
Lescar, Julien
Pervushin, Konstantin
Liang, Zhao-Xun
Title Solution structure of the PAS domain of a thermophilic YybT protein homolog reveals a potential ligand-binding site
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1067-8816
Publication date 2013-04
Sub-type Article (original research)
DOI 10.1074/jbc.M112.437764
Open Access Status File (Publisher version)
Volume 288
Issue 17
Start page 11949
End page 11959
Total pages 11
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Collection year 2014
Language eng
Abstract The Bacillus subtilis protein YybT (or GdpP) and its homologs were recently established as stress signaling proteins that exert their biological effect by degrading the bacterial messenger cyclic di-AMP. YybT homologs contain a small Per-ARNT-Sim (PAS) domain (-80 amino acids) that can bind b-type heme with 1:1 stoichiometry despite the small size of the domain and the lack of a conserved heme iron-coordinating residue. We determined the solution structure of the PAS domain of GtYybT from Geobacillus thermodenitrificans by NMR spectroscopy to further probe its function. The solution structure confirms that PAS GtYybT adopts the characteristic PAS fold composed of a five-stranded antiparallel β sheet and a few short α-helices. One α-helix and three central β-strands of PASGtYybT are noticeably shorter than those of the typical PAS domains. Despite the small size of the protein domain, a hydrophobic pocket is formed by the side chains of nonpolar residues stemming from the β-strands and α-helices. A set of residues in the vicinity of the pocket and in the C-terminal region at the dimeric interface exhibits perturbed NMR parameters in the presence of heme or zinc protoporphyrin. Together, the results unveil a compact PAS domain with a potential ligand-binding pocket and reinforce the view that the PASYybT domains function as regulatory domains in the modulation of cellular cyclic di-AMP concentration.
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Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Agriculture and Food Sciences
Queensland Alliance for Agriculture and Food Innovation
Official 2014 Collection
 
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