1lfo
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(New page: 200px<br /><applet load="1lfo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lfo, resolution 2.3Å" /> '''LIVER FATTY ACID BIND...)
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Revision as of 18:24, 20 November 2007
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LIVER FATTY ACID BINDING PROTEIN-OLEATE COMPLEX
Overview
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.
About this Structure
1LFO is a Single protein structure of sequence from Rattus norvegicus with ACE, OLA, BEO and UNX as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates., Thompson J, Winter N, Terwey D, Bratt J, Banaszak L, J Biol Chem. 1997 Mar 14;272(11):7140-50. PMID:9054409
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