Crystallization of a functionally intact Hsc70 chaperone

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Jianwen JiangRui Sousa

Abstract

Hsp70s are essential chaperones with roles in a variety of cellular processes and representatives in all kingdoms of life. They are comprised of a nucleotide-binding domain (NBD) and a protein substrate-binding domain (SBD). Structures of isolated NBDs and SBDs have been reported but, until recently, a functionally intact Hsp70 containing both the NBD and SBD has resisted structure determination. Here, it is reported that preparation of diffraction-quality crystals of functionally intact bovine Hsc70 required (i) deletion of part of the protein to reduce oligomerization, (ii) point mutations in the interface between the SBD and NBD and (iii) use of high concentrations of the structure-stabilizing agents glycerol and trimethylamine oxide (TMAO). The introduction of point mutations in interdomain interfaces and the use of the potent structure stabilizer TMAO may be generally useful in crystallization of multidomain proteins that exhibit interdomain motions.

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Citations

Jan 22, 2008·Proceedings of the National Academy of Sciences of the United States of America·Walid AwadLinda M Hendershot
Jun 19, 2010·Transgenic Research·Giampaolo BurianiSelene Baschieri
Apr 24, 2015·Journal of Cellular and Molecular Medicine·Teresa PasquaTommaso Angelone
Jul 17, 2007·Trends in Biochemical Sciences·Pierre Goloubinoff, Paolo De Los Rios
Jan 11, 2011·Nature Structural & Molecular Biology·Moritz MarcinowskiJohannes Buchner
Nov 13, 2007·Molecular Cell·Jianwen JiangRui Sousa

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