1G74

Toward changing specificity: adipocyte lipid binding protein mutant, oleic acid bound form

Summary for 1G74

• Entry DOI: 10.2210/pdb1g74/pdb
• Related: 1G7N
• Descriptor: ADIPOCYTE LIPID-BINDING PROTEIN, PHOSPHATE ION, OLEIC ACID, ... (4 entities in total)
• Functional Keywords: beta-barrel, fatty acid binding protein, protein engineering, fatty acid binding, lipid binding protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm: P04117
• Total number of polymer chains: 1
• Total formula weight: 14903.09

Authors

Reese, A.J.,Banaszak, L.J. (deposition date: 2000-11-08, release date: 2003-06-10, Last modification date: 2023-08-09)

Primary citation

Reese, A.J.,Banaszak, L.J.
Specificity determinants for lipids bound to beta-barrel proteins.
J.Lipid Res., 45:232-243, 2004

PubMed Abstract: The family of proteins accountable for the intracellular movement of lipids is characterized by a 10-stranded beta-barrel that forms an internalized cavity varying in size and binding preferences. The loop connecting beta-strands E and F (the fifth and sixth strands) is the most striking conformational difference between adipocyte lipid binding protein (ALBP; fatty acids) and cellular retinoic acid binding protein type I (CRABP I). A three-residue mutation was made in wild-type (WT)-ALBP [ALBP with a three-residue mutation (EF-ALBP)] to mimic CRABP I. Crystal structures of ligand-free and EF-ALBP with bound oleic acid were solved to resolutions of 1.5 A and 1.7 A, respectively, and compared with previous studies of WT-ALBP. The changes in three residues of one loop of the protein appear to have altered the positioning of the C18 fatty acid, as observed in the electron density of EF-ALBP. The crystallographic studies made it possible to compare the protein conformation and ligand positioning with those found in the WT protein. Although the cavity binding sites in both the retinoid and fatty acid binding proteins are irregular, the ligand atoms appear to favor a relatively planar region of the cavities. Preliminary chemical characterization of the mutant protein indicated changes in some binding properties and overall protein stability.

PubMed: 14594993
DOI: 10.1194/jlr.M300113-JLR200

Experimental method

X-RAY DIFFRACTION (1.7 Å)