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Publikācija: A Novel Zinc-Binding Fold in the Helicase Intreraction Domain of Bacillus Subtilis Dnai Helicase Loader

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Publikācijas valoda English (en)
Nosaukums oriģinālvalodā A Novel Zinc-Binding Fold in the Helicase Intreraction Domain of Bacillus Subtilis Dnai Helicase Loader
Pētniecības nozare 1. Dabaszinātnes
Pētniecības apakšnozare 1.4. Ķīmija
Autori Karin Loscha
Kristaps Jaudzems
Charikleia Ioannou
Xun-Cheng Su
Flynn R. Hill
Gottfried Otting
Nicholas Dixon
Edvards Liepiņš
Atslēgas vārdi chemistry ; bioinformatics and computational biology ; genetics and genomics ; molecular and cell biology
Anotācija 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.
DOI: 10.1093/nar/gkp092
Hipersaite: http://nar.oxfordjournals.org/content/37/7/2395 
Atsauce Loscha, K., Jaudzems, K., Ioannou, C., Su, X., Hill, F., Otting, G., Dixon, N., Liepiņš, E. A Novel Zinc-Binding Fold in the Helicase Intreraction Domain of Bacillus Subtilis Dnai Helicase Loader. Nucleic Acids Research, 2009, Vol.37, No.7, 2395.-2404.lpp. e-ISSN 1362-4962. ISSN 0305-1048. Pieejams: doi:10.1093/nar/gkp092
ID 7152