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TitleThe structure of the PA28-20S proteasome complex from Plasmodium falciparum and implications for proteostasis.
Journal, issue, pagesNat Microbiol, Vol. 4, Issue 11, Page 1990-2000, Year 2019
Publish dateAug 5, 2019
AuthorsStanley C Xie / Riley D Metcalfe / Eric Hanssen / Tuo Yang / David L Gillett / Andrew P Leis / Craig J Morton / Michael J Kuiper / Michael W Parker / Natalie J Spillman / Wilson Wong / Christopher Tsu / Lawrence R Dick / Michael D W Griffin / Leann Tilley /
PubMed AbstractThe activity of the proteasome 20S catalytic core is regulated by protein complexes that bind to one or both ends. The PA28 regulator stimulates 20S proteasome peptidase activity in vitro, but its ...The activity of the proteasome 20S catalytic core is regulated by protein complexes that bind to one or both ends. The PA28 regulator stimulates 20S proteasome peptidase activity in vitro, but its role in vivo remains unclear. Here, we show that genetic deletion of the PA28 regulator from Plasmodium falciparum (Pf) renders malaria parasites more sensitive to the antimalarial drug dihydroartemisinin, indicating that PA28 may play a role in protection against proteotoxic stress. The crystal structure of PfPA28 reveals a bell-shaped molecule with an inner pore that has a strong segregation of charges. Small-angle X-ray scattering shows that disordered loops, which are not resolved in the crystal structure, extend from the PfPA28 heptamer and surround the pore. Using single particle cryo-electron microscopy, we solved the structure of Pf20S in complex with one and two regulatory PfPA28 caps at resolutions of 3.9 and 3.8 Å, respectively. PfPA28 binds Pf20S asymmetrically, strongly engaging subunits on only one side of the core. PfPA28 undergoes rigid body motions relative to Pf20S. Molecular dynamics simulations support conformational flexibility and a leaky interface. We propose lateral transfer of short peptides through the dynamic interface as a mechanism facilitating the release of proteasome degradation products.
External linksPubMed:31384003 / Publisher's page
KeywordsArtemisinins / Cryoelectron Microscopy / Crystallography, X-Ray / Models, Molecular / Molecular Dynamics Simulation / Plasmodium falciparum / Proteasome Endopeptidase Complex / Protein Conformation / Protein Multimerization / Proteostasis / Protozoan Proteins / Scattering, Small Angle / X-Ray Diffraction / dihydroartemisinin / PROTEIN BINDING / 11S proteasome subunit / 11S regulatory particle / PA28 / REG / proteasome activator / hydrolase activator / HYDROLASE / proteasome / protease / 11S subunit / hydrolyse activator / complex
MethodsEM (single particle) / X-ray diffraction
Resolution3.1 - 4.6 A
Structure data

EMDB-20073:
Reconstruction of the Plasmodium falciparum 20S proteasome in complex with one PA28 activator prepared without chemical stabilisation

EMDB-9257:
The structure of the Plasmodium falciparum 20S proteasome in complex with two PA28 activators

EMDB-9258:
The structure of the Plasmodium falciparum 20S proteasome.

EMDB-9259:
The structure of the Plasmodium falciparum 20S proteasome in complex with one PA28 activator

PDB-6dfk:
Crystal structure of the 11S subunit of the Plasmodium falciparum proteasome, PA28

PDB-6muv:
The structure of the Plasmodium falciparum 20S proteasome in complex with two PA28 activators

PDB-6muw:
The structure of the Plasmodium falciparum 20S proteasome.

PDB-6mux:
The structure of the Plasmodium falciparum 20S proteasome in complex with one PA28 activator

Chemicals

ChemComp-SO4:
SULFATE ION / Sulfate

Source
  • plasmodium falciparum 3d7 (eukaryote)
  • plasmodium falciparum (isolate 3d7) (eukaryote)
  • plasmodium falciparum (malaria parasite P. falciparum)

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