5U2U

Crystal structure of the Hsp104 N-terminal domain from Saccharomyces cerevisiae

Summary for 5U2U

• Entry DOI: 10.2210/pdb5u2u/pdb
• Descriptor: Heat shock protein 104 (2 entities in total)
• Functional Keywords: saccharomyces cerevisiae, hsp104, n-terminal domain, protein binding
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 3
• Total formula weight: 56628.81

Authors

Wang, P.,Li, J.,Sha, B. (deposition date: 2016-11-30, release date: 2017-04-19, Last modification date: 2024-03-06)

Primary citation

Wang, P.,Li, J.,Weaver, C.,Lucius, A.,Sha, B.
Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 in dissolving prions.
Acta Crystallogr D Struct Biol, 73:365-372, 2017

PubMed Abstract: Hsp104 is a yeast member of the Hsp100 family which functions as a molecular chaperone to disaggregate misfolded polypeptides. To understand the mechanism by which the Hsp104 N-terminal domain (NTD) interacts with its peptide substrates, crystal structures of the Hsp104 NTDs from Saccharomyces cerevisiae (ScHsp104NTD) and Candida albicans (CaHsp104NTD) have been determined at high resolution. The structures of ScHsp104NTD and CaHsp104NTD reveal that the yeast Hsp104 NTD may utilize a conserved putative peptide-binding groove to interact with misfolded polypeptides. In the crystal structures ScHsp104NTD forms a homodimer, while CaHsp104NTD exists as a monomer. The consecutive residues Gln105, Gln106 and Lys107, and Lys141 around the putative peptide-binding groove mediate the monomer-monomer interactions within the ScHsp104NTD homodimer. Dimer formation by ScHsp104NTD suggests that the Hsp104 NTD may specifically interact with polyQ regions of prion-prone proteins. The data may reveal the mechanism by which Hsp104 NTD functions to suppress and/or dissolve prions.

PubMed: 28375147
DOI: 10.1107/S2059798317002662

Experimental method

X-RAY DIFFRACTION (2.541 Å)