2JMP
Structure for the N-terminus of chromosomal replication initiation protein dnaA from M. genitalium
Summary for 2JMP
Entry DOI | 10.2210/pdb2jmp/pdb |
Related | 1L8Q |
NMR Information | BMRB: 15055 |
Descriptor | Chromosomal replication initiator protein dnaA (1 entity in total) |
Functional Keywords | n-terminal, protein, structural genomics, psi, protein structure initiative, berkeley structural genomics center, bsgc, dna binding protein |
Biological source | Mycoplasma genitalium |
Total number of polymer chains | 1 |
Total formula weight | 12343.83 |
Authors | Lowery, T.J.,Pelton, J.G.,Wemmer, D.E.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2006-11-27, release date: 2007-07-17, Last modification date: 2024-05-08) |
Primary citation | Lowery, T.J.,Pelton, J.G.,Chandonia, J.M.,Kim, R.,Yokota, H.,Wemmer, D.E. NMR structure of the N-terminal domain of the replication initiator protein DnaA. J.Struct.Funct.Genom., 8:11-17, 2007 Cited by PubMed Abstract: 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 A 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. PubMed: 17680349DOI: 10.1007/s10969-007-9022-7 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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