Expression, refolding, and initial structural characterization of the Y. pestis Ail outer membrane protein in lipids
| Autor: | Jasmina Racic, Radhakrishnan Mahalakshmi, Leigh A. Plesniak, Candace Rypien, Yuan Yang, Francesca M. Marassi |
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| Rok vydání: | 2010 |
| Předmět: |
Protein Folding
Magnetic Resonance Spectroscopy Virulence Factors Yersinia pestis Molecular Sequence Data Biophysics Molecular Conformation Micelle Biochemistry Virulence factor Bacterial Adhesion Protein Structure Secondary Article 03 medical and health sciences Amino Acid Sequence Bilayer Lipid bilayer 030304 developmental biology Ail 0303 health sciences biology Sequence Homology Amino Acid 030306 microbiology Circular Dichroism Adhesion Cell Biology Gene Expression Regulation Bacterial Hydrogen-Ion Concentration biology.organism_classification Lipids Transmembrane protein NMR 3. Good health Bicelle Outer membrane protein Bacterial outer membrane Function (biology) Bacterial Outer Membrane Proteins |
| Zdroj: | Biochimica et biophysica acta. 1808(1) |
| ISSN: | 0006-3002 |
| Popis: | Ail is an outer membrane protein and virulence factor of Yersinia pestis, an extremely pathogenic, category A biothreat agent, responsible for precipitating massive human plague pandemics throughout history. Due to its key role in bacterial adhesion to host cells and bacterial resistance to host defense, Ail is a key target for anti-plague therapy. However, little information is available about the molecular aspects of its function and interactions with the human host, and the structure of Ail is not known. Here we describe the recombinant expression, purification, refolding, and sample preparation of Ail for solution and solid-state NMR structural studies in lipid micelles and lipid bilayers. The initial NMR and CD spectra show that Ail adopts a well-defined transmembrane β-sheet conformation in lipids. |
| Databáze: | OpenAIRE |
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