2c9o: Difference between revisions

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 functions, we, could only detect a marginal activity with the purified protein., Structural homology and DNA binding studies demonstrate that the second, domain, which is unique among AAA(+) proteins and not present in the, bacterial homolog RuvB, is a novel DNA/RNA-binding domain. We were able to, demonstrate that RuvBL1 interacted with single-stranded DNA/RNA and, double-stranded DNA. The structure of the RuvBL1.ADP complex, combined, with our biochemical results, suggest that although RuvBL1 has all the, structural characteristics of a molecular motor, even of an ATP-driven, helicase, one or more as yet undetermined cofactors are needed for its, enzymatic activity.

2C9O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ADP as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C9O OCA].  

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