2c9o
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3D STRUCTURE OF THE HUMAN RUVB-LIKE HELICASE RUVBL1
OverviewOverview
RuvBL1 is an evolutionarily highly conserved eukaryotic protein belonging, to the AAA(+)-family of ATPases (ATPase associated with diverse cellular, activities). It plays important roles in essential signaling pathways such, as the c-Myc and Wnt pathways in chromatin remodeling, transcriptional and, developmental regulation, and DNA repair and apoptosis. Herein we present, the three-dimensional structure of the selenomethionine variant of human, RuvBL1 refined using diffraction data to 2.2A of resolution. The crystal, structure of the hexamer is formed of ADP-bound RuvBL1 monomers. The, monomers contain three domains, of which the first and the third are, involved in ATP binding and hydrolysis. Although it has been shown that, ATPase activity of RuvBL1 is needed for several in vivo ... [(full description)]
About this StructureAbout this Structure
2C9O is a [Single protein] structure of sequence from [Homo sapiens] with ADP as [ligand]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of the human AAA+ protein RuvBL1., Matias PM, Gorynia S, Donner P, Carrondo MA, J Biol Chem. 2006 Dec 15;281(50):38918-29. Epub 2006 Oct 23. PMID:17060327
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