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PubMed · 9757124

Crystallographic characterization of Pap1-DNA complex.

Y Fujii·T Ohira·Y Kyougoku·T Toda·M Yanagida·T Hakoshima
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Abstract

Pap1 is a fission yeast transcription factor that activates genes related with resistance against staurosporine, a potent inhibitor of protein kinase C, and has been shown to be involved in cell growth, cell cycle, carcinogenesis and differentiation. Pap1 has the bZIP DNA-binding domain but binds to non-consensus DNA sequences for the bZIP motif. Highly ordered crystals of the DNA-binding domain complexed with a DNA fragment that has an ATF/CREB-like non-consensus sequence have been obtained. The crystals grew by the vapor-diffusion technique with polyethylene glycol 6000 and belong to space group R3 with a = b = 240.78, c = 43.85 A. A 2.0 A resolution data set was collected with a cryo-crystallographic technique.

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Basic-Leucine Zipper Transcription FactorsCrystallizationCrystallography, X-RayDNA, FungalDNA-Binding ProteinsFreezingFungal ProteinsMacromolecular SubstancesOligodeoxyribonucleotidesPancreatitis-Associated ProteinsProtein BindingProtein ConformationRecombinant Fusion ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsJournal ArticleResearch Support, Non-U.S. Gov't

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Y Fujii, T Ohira, Y Kyougoku, T Toda, M Yanagida, T Hakoshima. 1998-09-01. Crystallographic characterization of Pap1-DNA complex.. https://doi.org/10.1107/s0907444998003266

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