NMR structure of the N-terminal domain of the replication initiator protein DnaA
| Autor: | John-Marc Chandonia, David E. Wemmer, Jeffrey G. Pelton, Rosalind Kim, Hisao Yokota, Thomas J. Lowery |
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| Rok vydání: | 2007 |
| Předmět: |
DNA Replication
Magnetic Resonance Spectroscopy Protein Conformation Base pair Stereochemistry Molecular Sequence Data Mycoplasma genitalium Biochemistry Protein structure Bacterial Proteins Species Specificity SeqA protein domain Structural Biology Escherichia coli Genetics Amino Acid Sequence dnaB helicase biology DNA replication Helicase Hydrogen Bonding General Medicine DnaA Protein Structure Tertiary DNA-Binding Proteins Crystallography Residual dipolar coupling biology.protein Carrier Proteins DnaB Helicases |
| Zdroj: | Journal of Structural and Functional Genomics. 8:11-17 |
| ISSN: | 1570-0267 1345-711X |
| Popis: | DnaA is an essential component in the initiation of bacterial chromosomal replication. DnaA binds to a series of 9 base pair repeats leading to oligomerization, recruitment of the DnaBC helicase, and the assembly of the replication fork machinery. The structure of the N-terminal domain (residues 1-100) of DnaA from Mycoplasma genitalium was determined by NMR spectroscopy. The backbone r.m.s.d. for the first 86 residues was 0.6 +/- 0.2 Angstrom based on 742 NOE, 50 hydrogen bond, 46 backbone angle, and 88 residual dipolar coupling restraints. Ultracentrifugation studies revealed that the domain is monomeric in solution. Features on the protein surface include a hydrophobic cleft flanked by several negative residues on one side, and positive residues on the other. A negatively charged ridge is present on the opposite face of the protein. These surfaces may be important sites of interaction with other proteins involved in the replication process. Together, the structure and NMR assignments should facilitate the design of new experiments to probe the protein-protein interactions essential for the initiation of DNA replication. |
| Databáze: | OpenAIRE |
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