7tfm

Atomic Structure of the Leishmania spp. Hsp100 N-Domain

spinqualitylabelsall models 7tfm, resolution 1.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7tfm is a 1 chain structure with sequence from Leishmania mexicana MHOM/GT/2001/U1103. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.055Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E9ALU6_LEIMU 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Heat Shock Protein structures

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