@article{cafded9f3a8e424f9e082244f1abee22,
title = "Atomic structure of the Leishmania spp. Hsp100 N-domain",
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 {\AA} 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.",
keywords = "Hsp100, Leishmania, molecular chaperone, protein unfoldase",
author = "Mercado, {Jonathan M.} and Sukyeong Lee and Changsoo Chang and Nuri Sung and Lynn Soong and Andre Catic and Tsai, {Francis T.F.}",
note = "Funding Information: We thank J. Lee for help with cloning. This work was supported by the Welch Foundation (Q‐1530‐20190330), the National Institutes of Health (R01‐GM104980, R01‐GM142143, R01‐AI130126, and R01‐DK115454), and the Cancer Prevention and Research Institute of Texas (RR140038). Use of the Macromolecular X‐ray Crystallography Core at Baylor College of Medicine is supported in part by NIH grant S10‐OD030246. Use of the SBC beamlines at the Advanced Photon Source was supported by the US Department of Energy, Office of Science, Office of Basic Energy Sciences, under Contract No. DE‐AC02‐06CH11357. Jonathan M. Mercado was supported by a training fellowship from the Gulf Coast Consortia on the Houston Area Molecular Biophysics Program (T32‐GM008280). Publisher Copyright: {\textcopyright} 2022 Wiley Periodicals LLC.",
year = "2022",
month = jun,
doi = "10.1002/prot.26310",
language = "English (US)",
volume = "90",
pages = "1242--1246",
journal = "Proteins: Structure, Function and Bioinformatics",
issn = "0887-3585",
publisher = "Wiley-Liss Inc.",
number = "6",
}