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2JMP

Structure for the N-terminus of chromosomal replication initiation protein dnaA from M. genitalium

Summary for 2JMP
Entry DOI10.2210/pdb2jmp/pdb
Related1L8Q
NMR InformationBMRB: 15055
DescriptorChromosomal replication initiator protein dnaA (1 entity in total)
Functional Keywordsn-terminal, protein, structural genomics, psi, protein structure initiative, berkeley structural genomics center, bsgc, dna binding protein
Biological sourceMycoplasma genitalium
Total number of polymer chains1
Total formula weight12343.83
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 citationLowery, 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: 17680349
DOI: 10.1007/s10969-007-9022-7
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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