2K7R

N-terminal domain of the Bacillus subtilis helicase-loading protein DnaI

2K7R の概要

• エントリーDOI: 10.2210/pdb2k7r/pdb
• NMR情報: BMRB: 15926
• 分子名称: Primosomal protein dnaI, ZINC ION (2 entities in total)
• 機能のキーワード: dnai n-terminal domain, helicase-loading protein, atp-binding, dna replication, nucleotide-binding, primosome, replication
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12608.68

構造登録者

Loscha, K.V.,Jaudzems, K.,Ioannou, C.,Su, X.C.,Hill, F.R.,Otting, G.,Dixon, N.E.,Liepinsh, E. (登録日: 2008-08-19, 公開日: 2009-03-03, 最終更新日: 2024-05-15)

主引用文献

Loscha, K.V.,Jaudzems, K.,Ioannou, C.,Su, X.C.,Hill, F.R.,Otting, G.,Dixon, N.E.,Liepinsh, E.
A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loader
Nucleic Acids Res., 37:2395-2404, 2009

PubMed Abstract: The helicase loader protein DnaI (the Bacillus subtilis homologue of Escherichia coli DnaC) is required to load the hexameric helicase DnaC (the B. subtilis homologue of E. coli DnaB) onto DNA at the start of replication. While the C-terminal domain of DnaI belongs to the structurally well-characterized AAA+ family of ATPases, the structure of the N-terminal domain, DnaI-N, has no homology to a known structure. Three-dimensional structure determination by nuclear magnetic resonance (NMR) spectroscopy shows that DnaI presents a novel fold containing a structurally important zinc ion. Surface plasmon resonance experiments indicate that DnaI-N is largely responsible for binding of DnaI to the hexameric helicase from B. stearothermophilus, which is a close homologue of the corresponding much less stable B. subtilis helicase.

PubMed: 19255093
DOI: 10.1093/nar/gkp092

実験手法

SOLUTION NMR