2FT9

Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic acid


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.316 
  • R-Value Work: 0.258 
  • R-Value Observed: 0.260 

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This is version 1.3 of the entry. See complete history


Literature

Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic and oleic acid

Capaldi, S.Guariento, M.Perduca, M.Di Pietro, S.M.Santome, J.A.Monaco, H.L.

(2006) Proteins 64: 79-88

  • DOI: https://doi.org/10.1002/prot.20961
  • Primary Citation of Related Structures:  
    2FT9, 2FTB

  • PubMed Abstract: 

    The family of the liver bile acid-binding proteins (L-BABPs), formerly called liver basic fatty acid-binding proteins (Lb-FABPs) shares fold and sequence similarity with the paralogous liver fatty acid-binding proteins (L-FABPs) but has a different stoichiometry and specificity of ligand binding. This article describes the first X-ray structure of a member of the L-BABP family, axolotl (Ambystoma mexicanum) L-BABP, bound to two different ligands: cholic and oleic acid. The protein binds one molecule of oleic acid in a position that is significantly different from that of either of the two molecules that bind to rat liver FABP. The stoichiometry of binding of cholate is of two ligands per protein molecule, as observed in chicken L-BABP. The cholate molecule that binds buried most deeply into the internal cavity overlaps well with the analogous bound to chicken L-BABP, whereas the second molecule, which interacts with the first only through hydrophobic contacts, is more external and exposed to the solvent.


  • Organizational Affiliation

    Biocrystallography Laboratory, Department of Science & Technology, University of Verona, Verona, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Fatty acid-binding protein 2, liver125Ambystoma mexicanumMutation(s): 0 
UniProt
Find proteins for P81400 (Ambystoma mexicanum)
Explore P81400 
Go to UniProtKB:  P81400
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP81400
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.316 
  • R-Value Work: 0.258 
  • R-Value Observed: 0.260 
  • Space Group: I 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 73.664α = 90
b = 73.664β = 90
c = 61.546γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
CCP4data scaling
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-04-11
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-10-25
    Changes: Data collection, Database references, Derived calculations, Refinement description