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RUVBL

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The Crystal Structure of the Human AAA+ Protein RuvBL1

 

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 signalling pathways such as the c-Myc and Wnt pathways, in chromatin remodelling, in transcriptional and developmental regulation, and in DNA repair and apoptosis.

 

  

The crystal structure of RuvBL1 consists of hexamers, formed of ADP-bound monomers. The hexamers exhibit a central channel ca. 18 Å in diameter

The RuvBL1 monomer contains three domains, of which the first and the third are involved in ATP binding and hydrolysis.


 

 
Tube view of RuvBL1 in the region of the nucleotide-binding pocket.

View of the electrostatic potential of the RuvBL1 hexamer mapped at the molecular surface in the region of its central channel.

 

The structure of the RuvBL1/ADP complex, combined with our biochemical results, suggest that while RuvBL1 has all the structural characteristics of a molecular motor, even of an ATP-driven helicase, one or more as yet undetermined co-factors are needed for its enzymatic activity.


References:

P. M. Matias, S. Gorynia, P. Donner, M. A. Carrondo “Crystal Structure of the Human AAA+ Protein RuvBL1” (2006) J. Biol. Chem., JBC published October 23, 2006 as doi:10.1074/jbc.M605625200 [Accepted Manuscript]

S. Gorynia, P.M. Matias, S. Gonçalves, R. Coelho, G. Lopes, M. Thomaz, M. Huber, B. Haendler, P. Donner and M.A. Carrondo “Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1” (2006) Acta Crystallogr. F62:61-66

 

 

 

 

 

 

 

 

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