2C9O
3D Structure of the human RuvB-like helicase RuvBL1
Summary for 2C9O
| Entry DOI | 10.2210/pdb2c9o/pdb |
| Descriptor | RUVB-LIKE 1, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | hexameric helicase, aaa+-atpase, atp-binding, chromatin regulator, growth regulation, hydrolase, nuclear protein, dna recombination, transcription, transcription regulation, activator, helicase, nucleotide-binding |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 3 |
| Total formula weight | 152172.35 |
| Authors | Matias, P.M.,Gorynia, S.,Donner, P.,Carrondo, M.A. (deposition date: 2005-12-14, release date: 2006-10-23, Last modification date: 2024-05-08) |
| Primary citation | Matias, P.M.,Gorynia, S.,Donner, P.,Carrondo, M.A. Crystal structure of the human AAA+ protein RuvBL1. J. Biol. Chem., 281:38918-38929, 2006 Cited by PubMed Abstract: 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. PubMed: 17060327DOI: 10.1074/jbc.M605625200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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