5U2U

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

5U2U の概要

• エントリーDOI: 10.2210/pdb5u2u/pdb
• 分子名称: Heat shock protein 104 (2 entities in total)
• 機能のキーワード: saccharomyces cerevisiae, hsp104, n-terminal domain, protein binding
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 56628.81

構造登録者

Wang, P.,Li, J.,Sha, B. (登録日: 2016-11-30, 公開日: 2017-04-19, 最終更新日: 2024-03-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.541 Å)