7TFM

Atomic Structure of the Leishmania spp. Hsp100 N-Domain

7TFM の概要

• エントリーDOI: 10.2210/pdb7tfm/pdb
• 分子名称: ATP-dependent Clp protease subunit, heat shock protein 100 (HSP100), GLYCEROL (3 entities in total)
• 機能のキーワード: molecular chaperone, protein unfoldase, chaperone
• 由来する生物種: Leishmania mexicana MHOM/GT/2001/U1103
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17517.97

構造登録者

Mercado, J.M.,Lee, S.,Chang, C.,Sung, N.,Soong, L.,Catic, A.,Tsai, F.T.F. (登録日: 2022-01-06, 公開日: 2022-02-16, 最終更新日: 2023-10-18)

主引用文献

Mercado, J.M.,Lee, S.,Chang, C.,Sung, N.,Soong, L.,Catic, A.,Tsai, F.T.F.
Atomic structure of the Leishmania spp. Hsp100 N-domain.
Proteins, 90:1242-1246, 2022

PubMed Abstract: Hsp100 is an ATP-dependent unfoldase that promotes protein disaggregation or facilitates the unfolding of aggregation-prone polypeptides marked for degradation. Recently, new Hsp100 functions are emerging. In Plasmodium, an Hsp100 drives malaria protein export, presenting a novel drug target. Whether Hsp100 has a similar function in other protists is unknown. We present the 1.06 Å resolution crystal structure of the Hsp100 N-domain from Leishmania spp., the causative agent of leishmaniasis in humans. Our structure reveals a network of methionines and aromatic amino acids that define the putative substrate-binding site and likely evolved to protect Hsp100 from oxidative damage in host immune cells.

PubMed: 35122310
DOI: 10.1002/prot.26310

実験手法

X-RAY DIFFRACTION (1.055 Å)