7tfm

Publication Abstract from PubMed

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-A 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.

Atomic Structure of the Leishmania spp. Hsp100 N-Domain.,Mercado JM, Lee S, Chang C, Sung N, Soong L, Catic A, Tsai FTF Proteins. 2022 Feb 4. doi: 10.1002/prot.26310. PMID:35122310^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.