6HE5

20S core particle of PAN-proteasomes


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.12 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle.

Majumder, P.Rudack, T.Beck, F.Danev, R.Pfeifer, G.Nagy, I.Baumeister, W.

(2019) Proc Natl Acad Sci U S A 116: 534-539

  • DOI: https://doi.org/10.1073/pnas.1817752116
  • Primary Citation of Related Structures:  
    6HE4, 6HE5, 6HE7, 6HE8, 6HE9, 6HEA, 6HEC, 6HED

  • 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 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.


  • Organizational Affiliation

    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Proteasome subunit alpha
A, B, C, D, E
A, B, C, D, E, F, G
247Archaeoglobus fulgidus DSM 4304Mutation(s): 0 
Gene Names: psmAAF_0490
EC: 3.4.25.1
UniProt
Find proteins for O29760 (Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16))
Explore O29760 
Go to UniProtKB:  O29760
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO29760
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Proteasome subunit beta210Archaeoglobus fulgidus DSM 4304Mutation(s): 0 
Gene Names: psmBAF_0481
EC: 3.4.25.1
UniProt
Find proteins for Q9P996 (Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16))
Explore Q9P996 
Go to UniProtKB:  Q9P996
Entity Groups  
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UniProt GroupQ9P996
Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Proteasome-activating nucleotidase401Archaeoglobus fulgidus DSM 4304Mutation(s): 0 
Gene Names: panAF_1976
UniProt
Find proteins for O28303 (Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16))
Explore O28303 
Go to UniProtKB:  O28303
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO28303
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.12 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION2.1

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-12-26
    Type: Initial release
  • Version 1.1: 2019-01-16
    Changes: Data collection, Database references
  • Version 1.2: 2024-05-15
    Changes: Data collection, Database references