1LFO

LIVER FATTY ACID BINDING PROTEIN-OLEATE COMPLEX

Summary for 1LFO

• Entry DOI: 10.2210/pdb1lfo/pdb
• Descriptor: LIVER FATTY ACID BINDING PROTEIN, OLEIC ACID, BUTENOIC ACID, ... (5 entities in total)
• Functional Keywords: intracellular lipid transport protein, fatty acid binding protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: P02692
• Total number of polymer chains: 1
• Total formula weight: 14984.62

Authors

Thompson, J.,Winter, N.,Terwey, D.,Bratt, J.,Banaszak, L. (deposition date: 1996-12-09, release date: 1997-06-16, Last modification date: 2024-10-30)

Primary citation

Thompson, J.,Winter, N.,Terwey, D.,Bratt, J.,Banaszak, L.
The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates.
J.Biol.Chem., 272:7140-7150, 1997

PubMed Abstract: The crystal structure of the recombinant form of rat liver fatty acid-binding protein was completed to 2.3 A and refined to an R factor of 19.0%. The structural solution was obtained by molecular replacement using superimposed polyalanine coordinates of six intracellular lipid-binding proteins as a search probe. The entire amino acid sequence of rat liver fatty acid-binding protein along with an amino-terminal formyl-methionine was modeled in the crystal structure. In addition, the crystal was obtained in the presence of oleic acid, and the initial electron density clearly showed two fatty acid molecules bound within a central cavity. The carboxylate of one fatty acid molecule interacts with arginine 122 and is shielded from free solvent. It has an overall bent conformation. The more solvent-exposed carboxylate of the other oleate is located near the helix-turn-helix that caps one end of the beta-barrel, while the acyl chain lies in the interior. The cavity contains both polar and nonpolar residues but also shows extensive hydrophobic character around the nonpolar atoms of the ligands. The primary and secondary oleate binding sites appear to be totally interdependent, mainly because favorable hydrophobic interactions form between both aliphatic chains.

PubMed: 9054409
DOI: 10.1074/jbc.272.11.7140

Experimental method

X-RAY DIFFRACTION (2.3 Å)