Solution Structure of the PAS Domain of a Thermophilic YybT Protein Homolog Reveals a Potential Ligand-binding Site

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 h...

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Bibliographic Details
Published in:	The Journal of biological chemistry Vol. 288; no. 17; pp. 11949 - 11959
Main Authors:	Tan, Edward, Rao, Feng, Pasunooti, Swathi, Pham, Thi Huong, Soehano, Ishin, Turner, Mark S., Liew, Chong Wai, Lescar, Julien, Pervushin, Konstantin, Liang, Zhao-Xun
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 26-04-2013 American Society for Biochemistry and Molecular Biology
Subjects:	Antibiotic Resistance Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacterial Signal Transduction Cell Wall Cyclic Di-AMP Cyclic Nucleotides Dinucleoside Phosphates - chemistry Dinucleoside Phosphates - genetics Dinucleoside Phosphates - metabolism GdpP Geobacillus - chemistry Geobacillus - genetics Geobacillus - metabolism Heme Nuclear Magnetic Resonance, Biomolecular PAS Domain Protein Folding Protein Multimerization Protein Structure and Folding Protein Structure, Quaternary Protein Structure, Secondary Protein Structure, Tertiary YybT Cell Wall Cyclic Di-AMP Bacterial Signal Transduction Heme PAS Domain YybT Antibiotic Resistance GdpP Cyclic Nucleotides
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