Solution structure of DinI provides insight into its mode of RecA inactivation
| Autor: | R. D. Camerini-Otero, Ad Bax, Oleg N. Voloshin, Benjamin E. Ramirez |
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| Rok vydání: | 2000 |
| Předmět: |
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Molecular Protein Folding Magnetic Resonance Spectroscopy DNA Repair Protein Conformation Stereochemistry DNA repair Glutamic Acid medicine.disease_cause Antiparallel (biochemistry) Biochemistry Protein Structure Secondary chemistry.chemical_compound Protein structure Bacterial Proteins Escherichia coli medicine SOS response Molecular Biology Aspartic Acid Escherichia coli Proteins DNA Nuclear magnetic resonance spectroscopy Protein Structure Tertiary Rec A Recombinases Crystallography chemistry Mutagenesis Protein folding Software Protein Binding Research Article |
| Zdroj: | Protein Science. 9:2161-2169 |
| ISSN: | 1469-896X 0961-8368 |
| DOI: | 10.1110/ps.9.11.2161 |
| Popis: | The Escherichia coli RecA protein triggers both DNA repair and mutagenesis in a process known as the SOS response. The 81-residue E. coli protein DinI inhibits activity of RecA in vivo. The solution structure of DinI has been determined by multidimensional triple resonance NMR spectroscopy, using restraints derived from two sets of residual dipolar couplings, obtained in bicelle and phage media, supplemented with J couplings and a moderate number of NOE restraints. DinI has an alpha/beta fold comprised of a three-stranded beta-sheet and two alpha-helices. The beta-sheet topology is unusual: the central strand is flanked by a parallel and an antiparallel strand and the sheet is remarkably flat. The structure of DinI shows that six negatively charged Glu and Asp residues on DinI's kinked C-terminal alpha-helix form an extended, negatively charged ridge. We propose that this ridge mimics the electrostatic character of the DNA phospodiester backbone, thereby enabling DinI to compete with single-stranded DNA for RecA binding. Biochemical data confirm that DinI is able to displace ssDNA from RecA. |
| Databáze: | OpenAIRE |
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