Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	The structure of the PA28-20S proteasome complex from Plasmodium falciparum and implications for proteostasis.
Journal, issue, pages	Nat Microbiol, Vol. 4, Issue 11, Page 1990-2000, Year 2019
Publish date	Aug 5, 2019
Authors	Stanley 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 Abstract	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 ...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 links	Nat Microbiol / PubMed:31384003
Methods	EM (single particle) / X-ray diffraction
Resolution	3.1 - 4.6 Å
Structure data	EMDB-20073: Reconstruction of the Plasmodium falciparum 20S proteasome in complex with one PA28 activator prepared without chemical stabilisation Method: EM (single particle) / Resolution: 4.6 Å 9257 6muv EMDB-9257: The structure of the Plasmodium falciparum 20S proteasome in complex with two PA28 activators. PDB-6muv: The structure of the Plasmodium falciparum 20S proteasome in complex with two PA28 activators Method: EM (single particle) / Resolution: 3.8 Å 9258 6muw EMDB-9258, PDB-6muw: The structure of the Plasmodium falciparum 20S proteasome. Method: EM (single particle) / Resolution: 3.6 Å 9259 6mux EMDB-9259: The structure of the Plasmodium falciparum 20S proteasome in complex with one PA28 activator. PDB-6mux: The structure of the Plasmodium falciparum 20S proteasome in complex with one PA28 activator Method: EM (single particle) / Resolution: 3.9 Å PDB-6dfk: Crystal structure of the 11S subunit of the Plasmodium falciparum proteasome, PA28 Method: X-RAY DIFFRACTION / Resolution: 3.1 Å
Chemicals	ChemComp-SO4: SULFATE ION / Sulfate
Source	plasmodium falciparum 3d7 (eukaryote) plasmodium falciparum (isolate 3d7) (eukaryote) plasmodium falciparum (malaria parasite P. falciparum)
Keywords	PROTEIN BINDING / 11S proteasome subunit / 11S regulatory particle / PA28 / REG / proteasome activator / hydrolase activator / HYDROLASE / proteasome / protease / 11S subunit / hydrolyse activator / complex