Secondary structure and topology of Acanthamoeba profilin I as determined by heteronuclear nuclear magnetic resonance spectroscopy
| Autor: | Sharon J. Archer, Dennis A. Torchia, Thomas D. Pollard, Valda K. Vinson |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Magnetic Resonance Spectroscopy
Molecular Sequence Data Acanthamoeba macromolecular substances Antiparallel (biochemistry) Biochemistry Protein Structure Secondary Profilins Protein structure Contractile Proteins Escherichia coli Animals Amino Acid Sequence Protein secondary structure Actin biology Chemistry Microfilament Proteins Hydrogen Bonding Nuclear magnetic resonance spectroscopy Hydrogen-Ion Concentration Recombinant Proteins Models Structural Profilin Heteronuclear molecule biology.protein Biophysics Two-dimensional nuclear magnetic resonance spectroscopy |
| Zdroj: | Biochemistry. 32(26) |
| ISSN: | 0006-2960 |
| Popis: | The protein profilin binds to both actin and the head groups of poly)phosphoinositide)s and may regulate both actin assembly and the phosphoinositide signaling pathway. As a first step in understanding the activity of profilin at the molecular level, we have determined the secondary structure of Acanthamoeba profilin I in solution using multidimensional, heteronuclear NMR spectroscopy. Using a combination of triple-resonance (1H, 13C, 15N) experiments, we obtained virtually complete backbone and side-chain resonance assignments based solely on scalar couplings. 3D and 4D NOESY experiments were then used to determine the secondary structure and global fold of Acanthamoeba profilin I. The central feature of the protein structure is a five-stranded antiparallel beta-sheet flanked by three helices and a short two-stranded antiparallel beta-sheet. |
| Databáze: | OpenAIRE |
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