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Wiley, Angewandte Chemie International Edition, 5(54), p. 1508-1511, 2014

DOI: 10.1002/anie.201409830

Wiley, Angewandte Chemie, 5(127), p. 1528-1531, 2014

DOI: 10.1002/ange.201409830

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Water-Mediated Recognition of Simple Alkyl Chains by Heart-Type Fatty-Acid-Binding Protein**

Journal article published in 2014 by Shigeru Matsuoka, Shigeru Sugiyama, Daisuke Matsuoka, Mika Hirose, Sébastien Lethu, Hikaru Ano, Toshiaki Hara, Osamu Ichihara, S. Roy Kimura, S. Roy Kimura, Satoshi Murakami ORCID, Hanako Ishida, Eiichi Mizohata, Tsuyoshi Inoue, Michio Murata ORCID
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Abstract

Long-chain fatty acids (FAs) with low water solubility require fatty-acid-binding proteins (FABPs) to transport them from cytoplasm to the mitochondria for energy production. However, the precise mechanism by which these proteins recognize the various lengths of simple alkyl chains of FAs with similar high affinity remains unknown. To address this question, we employed a newly developed calorimetric method for comprehensively evaluating the affinity of FAs, sub-Angstrom X-ray crystallography to accurately determine their 3D structure, and energy calculations of the coexisting water molecules using the computer program WaterMap. Our results clearly showed that the heart-type FABP (FABP3) preferentially incorporates a U-shaped FA of C10–C18 using a lipid-compatible water cluster, and excludes longer FAs using a chain-length-limiting water cluster. These mechanisms could help us gain a general understanding of how proteins recognize diverse lipids with different chain lengths.