2JMP

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

2JMP の概要

• エントリーDOI: 10.2210/pdb2jmp/pdb
• 関連するPDBエントリー: 1L8Q
• NMR情報: BMRB: 15055
• 分子名称: Chromosomal replication initiator protein dnaA (1 entity in total)
• 機能のキーワード: n-terminal, protein, structural genomics, psi, protein structure initiative, berkeley structural genomics center, bsgc, dna binding protein
• 由来する生物種: Mycoplasma genitalium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12343.83

構造登録者

Lowery, T.J.,Pelton, J.G.,Wemmer, D.E.,Berkeley Structural Genomics Center (BSGC) (登録日: 2006-11-27, 公開日: 2007-07-17, 最終更新日: 2024-05-08)

主引用文献

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

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

実験手法

SOLUTION NMR