7TFM
Atomic Structure of the Leishmania spp. Hsp100 N-Domain
Summary for 7TFM
| Entry DOI | 10.2210/pdb7tfm/pdb |
| Descriptor | ATP-dependent Clp protease subunit, heat shock protein 100 (HSP100), GLYCEROL (3 entities in total) |
| Functional Keywords | molecular chaperone, protein unfoldase, chaperone |
| Biological source | Leishmania mexicana MHOM/GT/2001/U1103 |
| Total number of polymer chains | 1 |
| Total formula weight | 17517.97 |
| Authors | Mercado, J.M.,Lee, S.,Chang, C.,Sung, N.,Soong, L.,Catic, A.,Tsai, F.T.F. (deposition date: 2022-01-06, release date: 2022-02-16, Last modification date: 2023-10-18) |
| Primary citation | 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 Cited by 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: 35122310DOI: 10.1002/prot.26310 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.055 Å) |
Structure validation
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