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4tkh

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==The 0.93 angstrom X-ray structure of the human heart fatty acid-binding protein complexed with myristic acid==
==The 0.93 angstrom X-ray structure of the human heart fatty acid-binding protein complexed with myristic acid==
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<StructureSection load='4tkh' size='340' side='right' caption='[[4tkh]], [[Resolution|resolution]] 0.93&Aring;' scene=''>
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<StructureSection load='4tkh' size='340' side='right'caption='[[4tkh]], [[Resolution|resolution]] 0.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4tkh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TKH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TKH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4tkh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TKH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.93&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wbg|3wbg]], [[4tjz|4tjz]], [[4tkb|4tkb]], [[3wvm|3wvm]], [[4tkj|4tkj]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tkh OCA], [http://pdbe.org/4tkh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tkh RCSB], [http://www.ebi.ac.uk/pdbsum/4tkh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tkh ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4tkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tkh OCA], [https://pdbe.org/4tkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tkh RCSB], [https://www.ebi.ac.uk/pdbsum/4tkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tkh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FABPH_HUMAN FABPH_HUMAN]] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
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[https://www.uniprot.org/uniprot/FABPH_HUMAN FABPH_HUMAN] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Water-mediated recognition of simple alkyl chains by heart-type Fatty-Acid-binding protein.,Matsuoka S, Sugiyama S, Matsuoka D, Hirose M, Lethu S, Ano H, Hara T, Ichihara O, Kimura SR, Murakami S, Ishida H, Mizohata E, Inoue T, Murata M Angew Chem Int Ed Engl. 2015 Jan 26;54(5):1508-11. doi: 10.1002/anie.201409830., Epub 2014 Dec 9. PMID:25491543<ref>PMID:25491543</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4tkh" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Sorting nexin|Sorting nexin]]
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*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Hara, T]]
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[[Category: Homo sapiens]]
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[[Category: Hirose, M]]
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[[Category: Large Structures]]
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[[Category: Inoue, T]]
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[[Category: Hara T]]
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[[Category: Ishida, H]]
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[[Category: Hirose M]]
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[[Category: Kakinouchi, K]]
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[[Category: Inoue T]]
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[[Category: Matsuoka, D]]
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[[Category: Ishida H]]
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[[Category: Matsuoka, S]]
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[[Category: Kakinouchi K]]
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[[Category: Mizohata, E]]
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[[Category: Matsuoka D]]
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[[Category: Murakami, S]]
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[[Category: Matsuoka S]]
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[[Category: Murata, M]]
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[[Category: Mizohata E]]
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[[Category: Sugiyama, S]]
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[[Category: Murakami S]]
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[[Category: Antiparallel beta barrel]]
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[[Category: Murata M]]
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[[Category: Fatty acid-binding protein]]
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[[Category: Sugiyama S]]
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[[Category: Human heart]]
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[[Category: Lipid binding protein]]
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[[Category: Myristic acid]]
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Current revision

The 0.93 angstrom X-ray structure of the human heart fatty acid-binding protein complexed with myristic acid

PDB ID 4tkh

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