1F2J

CRYSTAL STRUCTURE ANALYSIS OF ALDOLASE FROM T. BRUCEI


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.199 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases.

Chudzik, D.M.Michels, P.A.de Walque, S.Hol, W.G.

(2000) J Mol Biol 300: 697-707

  • DOI: https://doi.org/10.1006/jmbi.2000.3910
  • Primary Citation of Related Structures:  
    1EPX, 1F2J

  • PubMed Abstract: 

    Trypanosomatids, unicellular organisms responsible for several global diseases, contain unique organelles called glycosomes in which the first seven glycolytic enzymes are sequestered. We report the crystal structures of glycosomal fructose-1,6-bisphosphate aldolase from two major tropical pathogens, Trypanosoma brucei and Leishmania mexicana, the causative agents of African sleeping sickness and one form of leishmaniasis, respectively. Unlike mammalian aldolases, the T. brucei and L. mexicana aldolases contain nonameric N-terminal type 2 peroxisomal targeting signals (PTS2s) to direct their import into the glycosome. In both tetrameric trypanosomatid aldolases, the PTS2s from two different subunits form two closely intertwined structures. These "PTS2 dimers", which have very similar conformations in the two aldolase structures, are the first reported conformations of a glycosomal or peroxisomal PTS2, and provide opportunities for the design of trypanocidal compounds.


  • Organizational Affiliation

    Departments of Biological Structure and Biochemistry Biomolecular Structure Center, University of Washington, Seattle, WA, 98195-7742, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
FRUCTOSE-BISPHOSPHATE ALDOLASE, GLYCOSOMAL370Trypanosoma bruceiMutation(s): 0 
EC: 4.1.2.13
UniProt
Find proteins for P07752 (Trypanosoma brucei brucei)
Explore P07752 
Go to UniProtKB:  P07752
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP07752
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.199 
  • Space Group: I 4 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 209.66α = 90
b = 209.66β = 90
c = 209.66γ = 90
Software Package:
Software NamePurpose
AMoREphasing
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-07-13
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2018-06-06
    Changes: Advisory, Data collection, Derived calculations
  • Version 1.4: 2023-08-09
    Changes: Data collection, Database references, Refinement description