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	Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 116, Issue 2, Page 534-539, Year 2019
Publish date	Jan 8, 2019
Authors	Parijat Majumder / Till Rudack / Florian Beck / Radostin Danev / Günter Pfeifer / István Nagy / Wolfgang Baumeister /
PubMed Abstract	Proteasomes occur in all three domains of life, and are the principal molecular machines for the regulated degradation of intracellular proteins. They play key roles in the maintenance of protein ...Proteasomes occur in all three domains of life, and are the principal molecular machines for the regulated degradation of intracellular proteins. They play key roles in the maintenance of protein homeostasis, and control vital cellular processes. While the eukaryotic 26S proteasome is extensively characterized, its putative evolutionary precursor, the archaeal proteasome, remains poorly understood. The primordial archaeal proteasome consists of a 20S proteolytic core particle (CP), and an AAA-ATPase module. This minimal complex degrades protein unassisted by non-ATPase subunits that are present in a 26S proteasome regulatory particle (RP). Using cryo-EM single-particle analysis, we determined structures of the archaeal CP in complex with the AAA-ATPase PAN (proteasome-activating nucleotidase). Five conformational states were identified, elucidating the functional cycle of PAN, and its interaction with the CP. Coexisting nucleotide states, and correlated intersubunit signaling features, coordinate rotation of the PAN-ATPase staircase, and allosterically regulate N-domain motions and CP gate opening. These findings reveal the structural basis for a sequential around-the-ring ATPase cycle, which is likely conserved in AAA-ATPases.
External links	Proc Natl Acad Sci U S A / PubMed:30559193 / PubMed Central
Methods	EM (single particle)
Resolution	3.69 - 7.04 Å
Structure data	0209 6he4 EMDB-0209, PDB-6he4: AAA-ATPase ring of PAN-proteasomes Method: EM (single particle) / Resolution: 4.85 Å 0210 6he5 EMDB-0210, PDB-6he5: 20S core particle of PAN-proteasomes Method: EM (single particle) / Resolution: 4.12 Å 0211 6he7 EMDB-0211, PDB-6he7: 20S proteasome from Archaeoglobus fulgidus Method: EM (single particle) / Resolution: 3.69 Å 0212 6he8 EMDB-0212, PDB-6he8: PAN-proteasome in state 1 Method: EM (single particle) / Resolution: 6.86 Å 0213 6he9 EMDB-0213, PDB-6he9: PAN-proteasome in state 2 Method: EM (single particle) / Resolution: 6.35 Å 0214 6hea EMDB-0214, PDB-6hea: PAN-proteasome in state 3 Method: EM (single particle) / Resolution: 7.04 Å 0215 6hec EMDB-0215, PDB-6hec: PAN-proteasome in state 4 Method: EM (single particle) / Resolution: 6.95 Å 0216 6hed EMDB-0216, PDB-6hed: PAN-proteasome in state 5 Method: EM (single particle) / Resolution: 6.95 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM
Source	archaeoglobus fulgidus dsm 4304 (archaea) archaeoglobus fulgidus (strain atcc 49558 / vc-16 / dsm 4304 / jcm 9628 / nbrc 100126) (archaea)
Keywords	HYDROLASE / PAN / Proteasome / AAA-ATPase / Archaea