The crystal structure of the molecular machine RuvBL1/RuvBL2 complex reveals a dodecamer consisting of two heterohexameric rings with alternating RuvBLl and RuvBL2 monomers bound to ADP/ATP. Our structural, biochemical and SAXS results give relevant insights into the assembly and illuminate the mechanism of how these proteins might exert their activities.
References
P. M. Matias, S. Gorynia, P. Donner, M. A. Carrondo, “Crystal Structure of the Human AAA+ Protein RuvBL1”, J. Biol. Chem. (2006) 281, 38918-38929
S. Gorynia, T. M. Bandeiras, F. G. Pinho, C. E. McVey, C. Vonrhein, A. Round, D. I. Svergun, P. Donner, P. M. Matias and M. A. Carrondo “Structural and functional insights into a dodecameric molecular machine – The RuvBL1/RuvBL2 complex”, submitted.
Legend:The crystal structure of RuvBL1 consists of hexamers, formed of ADP-bound monomers. The hexamers exhibit a central channel ca. 18 Å in diameter
