6Z46

Structure of the S. acidocaldarius 20S proteasome (Saci0613/Saci0662)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.70 Å
  • R-Value Free: 0.334 
  • R-Value Work: 0.287 
  • R-Value Observed: 0.290 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The proteasome controls ESCRT-III-mediated cell division in an archaeon.

Tarrason Risa, G.Hurtig, F.Bray, S.Hafner, A.E.Harker-Kirschneck, L.Faull, P.Davis, C.Papatziamou, D.Mutavchiev, D.R.Fan, C.Meneguello, L.Arashiro Pulschen, A.Dey, G.Culley, S.Kilkenny, M.Souza, D.P.Pellegrini, L.de Bruin, R.A.M.Henriques, R.Snijders, A.P.Saric, A.Lindas, A.C.Robinson, N.P.Baum, B.

(2020) Science 369

  • DOI: https://doi.org/10.1126/science.aaz2532
  • Primary Citation of Related Structures:  
    6Z46

  • PubMed Abstract: 

    Sulfolobus acidocaldarius is the closest experimentally tractable archaeal relative of eukaryotes and, despite lacking obvious cyclin-dependent kinase and cyclin homologs, has an ordered eukaryote-like cell cycle with distinct phases of DNA replication and division. Here, in exploring the mechanism of cell division in S. acidocaldarius , we identify a role for the archaeal proteasome in regulating the transition from the end of one cell cycle to the beginning of the next. Further, we identify the archaeal ESCRT-III homolog, CdvB, as a key target of the proteasome and show that its degradation triggers division by allowing constriction of the CdvB1:CdvB2 ESCRT-III division ring. These findings offer a minimal mechanism for ESCRT-III-mediated membrane remodeling and point to a conserved role for the proteasome in eukaryotic and archaeal cell cycle control.


  • Organizational Affiliation

    MRC-Laboratory for Molecular Cell Biology, University College London (UCL), London, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Proteasome subunit alpha242Sulfolobus acidocaldariusMutation(s): 0 
Gene Names: psmAATY89_03330ATZ20_06355
EC: 3.4.25.1
UniProt
Find proteins for Q4JB24 (Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770))
Explore Q4JB24 
Go to UniProtKB:  Q4JB24
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ4JB24
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Proteasome subunit beta198Sulfolobus acidocaldariusMutation(s): 0 
Gene Names: psmBATY89_03090ATZ20_06115
EC: 3.4.25.1
UniProt
Find proteins for Q4JAY3 (Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770))
Explore Q4JAY3 
Go to UniProtKB:  Q4JAY3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ4JAY3
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.70 Å
  • R-Value Free: 0.334 
  • R-Value Work: 0.287 
  • R-Value Observed: 0.290 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 108.287α = 90
b = 193.654β = 90
c = 323.671γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
PDB_EXTRACTdata extraction
XDSdata reduction
Aimlessdata scaling
PHENIXmodel building
PHENIXphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Isaac Newton TrustUnited Kingdom--
Biotechnology and Biological Sciences Research Council (BBSRC)United Kingdom--

Revision History  (Full details and data files)

  • Version 1.0: 2020-08-05
    Type: Initial release
  • Version 1.1: 2020-08-12
    Changes: Author supporting evidence, Database references
  • Version 1.2: 2020-08-19
    Changes: Database references
  • Version 1.3: 2024-01-24
    Changes: Data collection, Database references, Refinement description