3D2F

Crystal structure of a complex of Sse1p and Hsp70

Summary for 3D2F

• Entry DOI: 10.2210/pdb3d2f/pdb
• Related: 3D2E
• Descriptor: Heat shock protein homolog SSE1, Heat shock 70 kDa protein 1, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: nucleotide exchange factor, protein folding, atp-binding, calmodulin-binding, chaperone, nucleotide-binding, phosphoprotein, stress response
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); More
• Cellular location: Cytoplasm : P32589
• Total number of polymer chains: 4
• Total formula weight: 236111.54

Authors

Polier, S.,Bracher, A. (deposition date: 2008-05-08, release date: 2008-06-17, Last modification date: 2023-08-30)

Primary citation

Polier, S.,Dragovic, Z.,Hartl, F.U.,Bracher, A.
Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding.
Cell(Cambridge,Mass.), 133:1068-1079, 2008

PubMed Abstract: Protein folding by Hsp70 is tightly controlled by cochaperones, including J-domain proteins that trigger ATP hydrolysis and nucleotide exchange factors (NEFs) that remove ADP from Hsp70. Here we present the crystal structure of the yeast NEF Sse1p (Hsp110) in complex with the nucleotide-binding domain (NBD) of Hsp70. Hsp110 proteins are homologous to Hsp70s and consist of an NBD, a beta sandwich domain, and a three helix bundle domain (3HBD). In the complex, the NBD of Sse1p is ATP bound, and together with the 3HBD it embraces the NBD of Hsp70, inducing opening and the release of bound ADP from Hsp70. Mutations that abolish NEF activity are lethal, thus defining nucleotide exchange on Hsp70 as an essential function of Sse1p. Our data suggest that Sse1p does not employ the nucleotide-dependent allostery and peptide-binding mode of canonical Hsp70s, and that direct interactions of substrate with Sse1p may support Hsp70-assisted protein folding in a cooperative process.

PubMed: 18555782
DOI: 10.1016/j.cell.2008.05.022

Experimental method

X-RAY DIFFRACTION (2.3 Å)