6jl3 | pdb_00006jl3

Crystal Structure of the UBL domain of Plasmodium Falciparum Dsk2

spinqualitylabelsall models 6jl3, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jl3 is a 1 chain structure with sequence from Plasmodium falciparum 3D7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.303Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8IIM8_PLAF7 Publication Abstract from PubMed One of the pathways by which proteins are targeted for degradation by the proteasome involve transport by shuttle proteins to proteasomal receptors. The malaria parasite Plasmodium falciparum has recently been found to possess a similar pathway, with the shuttle protein PfDsk2 being the major player. In this study, we have demonstrated how PfDsk2 and its recognition by proteasomal receptors differ from the mammalian system. Our crystal structure of unbound PfDsk2 UBL domain at 1.30A revealed an additional 310-helix compared to the human homolog, as well as a few significant differences in its putative binding interface with the proteasome receptors, PfRpn10 and PfRpn13. Moreover, the non-binding face of UBL showed a reversal of surface charge compared to HsDsk2 shuttle protein, instead resembling HOIL-like E3 ligase UBL domain. The affinity of the interaction with the proteasomal receptors remained similar to the human system, and dissociation constants of the same order of magnitude. On the other hand, we have found evidence of a novel interaction between PfRpn13(DEUBAD) with the PfDsk2(UBL) suggesting that PfDsk2 may work in cooperation with deubiquitinating enzymes for proofreading ubiquitinated substrates. Our study provides the first molecular look at shuttle proteins in Apicomplexan parasites and hints at how their interaction landscape might be broader than what we may expect. The recognition of proteasomal receptors by Plasmodium falciparum DSK2.,Gupta I, Khan S Mol Biochem Parasitol. 2020 Feb 11;236:111266. doi:, 10.1016/j.molbiopara.2020.111266. PMID:32057831 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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