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Structure paper

TitleCryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 116, Issue 2, Page 534-539, Year 2019
Publish dateJan 8, 2019
AuthorsParijat Majumder / Till Rudack / Florian Beck / Radostin Danev / Günter Pfeifer / István Nagy / Wolfgang Baumeister /
PubMed AbstractProteasomes 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 linksProc Natl Acad Sci U S A / PubMed:30559193 / PubMed Central
MethodsEM (single particle)
Resolution3.69 - 7.04 Å
Structure data

EMDB-0209, PDB-6he4:
AAA-ATPase ring of PAN-proteasomes
Method: EM (single particle) / Resolution: 4.85 Å

EMDB-0210, PDB-6he5:
20S core particle of PAN-proteasomes
Method: EM (single particle) / Resolution: 4.12 Å

EMDB-0211, PDB-6he7:
20S proteasome from Archaeoglobus fulgidus
Method: EM (single particle) / Resolution: 3.69 Å

EMDB-0212, PDB-6he8:
PAN-proteasome in state 1
Method: EM (single particle) / Resolution: 6.86 Å

EMDB-0213, PDB-6he9:
PAN-proteasome in state 2
Method: EM (single particle) / Resolution: 6.35 Å

EMDB-0214, PDB-6hea:
PAN-proteasome in state 3
Method: EM (single particle) / Resolution: 7.04 Å

EMDB-0215, PDB-6hec:
PAN-proteasome in state 4
Method: EM (single particle) / Resolution: 6.95 Å

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 molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • archaeoglobus fulgidus dsm 4304 (archaea)
  • archaeoglobus fulgidus (strain atcc 49558 / vc-16 / dsm 4304 / jcm 9628 / nbrc 100126) (archaea)
KeywordsHYDROLASE / PAN / Proteasome / AAA-ATPase / Archaea

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