4TKB
The 0.86 angstrom X-ray structure of the human heart fatty acid-binding protein complexed with lauric acid
Summary for 4TKB
| Entry DOI | 10.2210/pdb4tkb/pdb |
| Related | 3wbg 3WVM 4TJZ 4TKH 4TKJ 4WBK |
| Descriptor | Fatty acid-binding protein, heart, LAURIC ACID, HEXAETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | human, fatty acid-binding protein, antiparallel beta barrel, lipid binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 15644.00 |
| Authors | Sugiyama, S.,Matsuoka, S.,Mizohata, E.,Matsuoka, D.,Ishida, H.,Hirose, M.,Kakinouchi, K.,Hara, T.,Murakami, S.,Inoue, T.,Murata, M. (deposition date: 2014-05-26, release date: 2015-01-28, Last modification date: 2024-03-20) |
| Primary citation | Matsuoka, S.,Sugiyama, S.,Matsuoka, D.,Hirose, M.,Lethu, S.,Ano, H.,Hara, T.,Ichihara, O.,Kimura, S.R.,Murakami, S.,Ishida, H.,Mizohata, E.,Inoue, T.,Murata, M. Water-mediated recognition of simple alkyl chains by heart-type Fatty-Acid-binding protein Angew.Chem.Int.Ed.Engl., 54:1508-1511, 2015 Cited by PubMed 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. PubMed: 25491543DOI: 10.1002/anie.201409830 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.86 Å) |
Structure validation
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