3D2E: Crystal Structure Of A Complex Of Sse1p And Hsp70, Selenomethionine- Labeled Crystals

Citation:
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.
PDB ID: 3D2EDownload
MMDB ID: 65012
PDB Deposition Date: 2008/5/8
Updated in MMDB: 2011/10
Experimental Method:
x-ray diffraction
Resolution: 2.35  Å
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 3D2E: dimeric; determined by author
Molecular Components in 3D2E
Label Count Molecule
Proteins (2 molecules)
1
Heat Shock Protein Homolog Sse1(Gene symbol: SSE1)
Molecule annotation
1
Heat Shock 70 KDA Protein 1
Molecule annotation
Chemicals (3 molecules)
1
1
2
1
3
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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