Atomic structure of the Leishmania spp. Hsp100 N-domain

被引：1

作者：

Mercado, Jonathan M. ^{[1
]}

Lee, Sukyeong ^{[2
,3
]}

Chang, Changsoo ^{[4
]}

Sung, Nuri ^{[3
]}

Soong, Lynn ^{[5
]}

Catic, Andre ^{[1
,6
]}

Tsai, Francis T. F. ^{[1
,3
,7
]}

机构：

[1] Baylor Coll Med, Dept Mol & Cellular Biol, Houston, TX 77030 USA

[2] Baylor Coll Med, Adv Technol Core Macromol Xray Crystallog, Houston, TX 77030 USA

[3] Baylor Coll Med, Dept Biochem & Mol Biol, Houston, TX 77030 USA

[4] Argonne Natl Lab, Xray Sci Div, Struct Biol Ctr, 9700 S Cass Ave, Argonne, IL 60439 USA

[5] Univ Texas Med Branch, Inst Human Infect & Immun, Dept Microbiol & Immunol, Galveston, TX 77555 USA

[6] Baylor Coll Med, Huffington Ctr Aging, Houston, TX 77030 USA

[7] Baylor Coll Med, Dept Mol Virol & Microbiol, Houston, TX 77030 USA

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2022年 / 90卷 / 06期

基金：

美国国家卫生研究院;

关键词：

Hsp100; Leishmania; molecular chaperone; protein unfoldase;

D O I：

10.1002/prot.26310

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 angstrom 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.

引用

页码：1242 / 1246

页数：5