2W2U

STRUCTURAL INSIGHT INTO THE INTERACTION BETWEEN ARCHAEAL ESCRT-III AND AAA-ATPASE

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.225 
  • R-Value Observed: 0.227 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

A Role for the Escrt System in Cell Division in Archaea.

Samson, R.Y., Obita, T., Freund, S.M., Williams, R.L., Bell, S.D.

(2008) Science 322: 1710

  • DOI: https://doi.org/10.1126/science.1165322
  • Primary Citation of Related Structures:  
    2W2U

  • PubMed Abstract: 

    Archaea are prokaryotic organisms that lack endomembrane structures. However, a number of hyperthermophilic members of the Kingdom Crenarchaea, including members of the Sulfolobus genus, encode homologs of the eukaryotic endosomal sorting system components Vps4 and ESCRT-III (endosomal sorting complex required for transport-III). We found that Sulfolobus ESCRT-III and Vps4 homologs underwent regulation of their expression during the cell cycle. The proteins interacted and we established the structural basis of this interaction. Furthermore, these proteins specifically localized to the mid-cell during cell division. Overexpression of a catalytically inactive mutant Vps4 in Sulfolobus resulted in the accumulation of enlarged cells, indicative of failed cell division. Thus, the archaeal ESCRT system plays a key role in cell division.

    • Organizational Affiliation: 

    Medical Research Council (MRC) Cancer Cell Unit, Hills Road, Cambridge CB2 0XZ, UK.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HYPOTHETICAL P60 KATANIN
A, B
83Sulfolobus acidocaldariusMutation(s): 0 
UniProt
Find proteins for Q877H3 (Sulfolobus acidocaldarius)
Explore Q877H3 
Go to UniProtKB:  Q877H3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ877H3
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
CONSERVED ARCHAEAL PROTEIN
C, D
14Sulfolobus acidocaldariusMutation(s): 0 
UniProt
Find proteins for Q4J924 (Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770))
Explore Q4J924 
Go to UniProtKB:  Q4J924
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ4J924
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.225 
  • R-Value Observed: 0.227 
  • Space Group: P 43
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.855α = 90
b = 49.855β = 90
c = 107.672γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-07-14
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-01-24
    Changes: Source and taxonomy
  • Version 1.4: 2023-12-13
    Changes: Data collection, Database references, Other, Refinement description