1HBK

Acyl-CoA binding protein from Plasmodium falciparum


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.198 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.6 of the entry. See complete history


Literature

Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein.

van Aalten, D.M.Milne, K.G.Zou, J.Y.Kleywegt, G.J.Bergfors, T.Ferguson, M.A.Knudsen, J.Jones, T.A.

(2001) J Mol Biol 309: 181-192

  • DOI: https://doi.org/10.1006/jmbi.2001.4749
  • Primary Citation of Related Structures:  
    1HB6, 1HB8, 1HBK

  • PubMed Abstract: 

    Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA molecules in the cell and plays a role in fatty acid metabolism. The biochemical properties of Plasmodium falciparum ACBP are described together with the 2.0 A resolution crystal structures of a P. falciparum ACBP-acyl-CoA complex and of bovine ACBP in two crystal forms. Overall, the bovine ACBP crystal structures are similar to the NMR structures published previously; however, the bovine and parasite ACBP structures are less similar. The parasite ACBP is shown to have a different ligand-binding pocket, leading to an acyl-CoA binding specificity different from that of bovine ACBP. Several non-conservative differences in residues that interact with the ligand were identified between the mammalian and parasite ACBPs. These, together with measured binding-specificity differences, suggest that there is a potential for the design of molecules that might selectively block the acyl-CoA binding site.


  • Organizational Affiliation

    Wellcome Trust Biocentre, Department of Biochemistry University of Dundee, Scotland. [email protected]


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ACYL-COA BINDING PROTEIN89Plasmodium falciparumMutation(s): 0 
UniProt
Find proteins for Q8IK57 (Plasmodium falciparum (isolate 3D7))
Explore Q8IK57 
Go to UniProtKB:  Q8IK57
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8IK57
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.198 
  • Space Group: P 43
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 48.665α = 90
b = 48.665β = 90
c = 48.411γ = 90
Software Package:
Software NamePurpose
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-05-15
    Type: Initial release
  • Version 1.1: 2011-05-07
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-01-31
    Changes: Advisory, Database references, Structure summary
  • Version 1.4: 2019-07-24
    Changes: Data collection
  • Version 1.5: 2019-10-09
    Changes: Data collection, Other
  • Version 1.6: 2024-05-08
    Changes: Advisory, Data collection, Database references, Derived calculations