1TBE

STRUCTURE OF TETRAUBIQUITIN SHOWS HOW MULTIUBIQUITIN CHAINS CAN BE FORMED


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Work: 0.184 
  • R-Value Observed: 0.184 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structure of tetraubiquitin shows how multiubiquitin chains can be formed.

Cook, W.J.Jeffrey, L.C.Kasperek, E.Pickart, C.M.

(1994) J Mol Biol 236: 601-609

  • DOI: https://doi.org/10.1006/jmbi.1994.1169
  • Primary Citation of Related Structures:  
    1TBE

  • PubMed Abstract: 

    Eukaryotic proteins are targeted for degradation by covalent ligation of multiubiquitin chains. In these multiubiquitin chains, successive ubiquitins are linked by an isopeptide bond involving the side chain of Lys48 and the carboxyl group of the C-terminus (Gly76). The crystal structure of a tetraubiquitin chain (Ub4) has been determined and refined at 2.4 A resolution. The molecule exhibits both translational and 2-fold rotational symmetry; each pair of (rotationally symmetric) ubiquitin molecules in Ub4 is related to the next pair by a simple translation. The 2-fold symmetry in each pair of ubiquitin molecules is quite different from the 2-fold symmetry observed in the previously determined structure of isolated diubiquitin. There are multiple hydrophilic contacts among the four ubiquitin molecules, but the hydrophobic surface formed in the middle of diubiquitin is not seen. The structure of the tetraubiquitin chain demonstrates how a multiubiquitin chain of any length can be formed.


  • Organizational Affiliation

    Department of Pathology, University of Alabama at Birmingham 35294.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TETRAUBIQUITIN
A, B
76Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P0CG48 (Homo sapiens)
Explore P0CG48 
Go to UniProtKB:  P0CG48
PHAROS:  P0CG48
GTEx:  ENSG00000150991 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0CG48
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Work: 0.184 
  • R-Value Observed: 0.184 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 24.1α = 90
b = 57β = 94.06
c = 47γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
PROLSQrefinement
X-PLORrefinement
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1994-01-31
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-07-17
    Changes: Data collection, Derived calculations, Other, Refinement description
  • Version 1.4: 2019-08-14
    Changes: Data collection, Refinement description