4tkb: Difference between revisions
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''' | ==The 0.86 angstrom X-ray structure of the human heart fatty acid-binding protein complexed with lauric acid== | ||
<StructureSection load='4tkb' size='340' side='right' caption='[[4tkb]], [[Resolution|resolution]] 0.86Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4tkb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TKB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TKB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAO:LAURIC+ACID'>DAO</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wbg|3wbg]], [[3wvm|3wvm]], [[4tjz|4tjz]], [[4tkh|4tkh]], [[4tkj|4tkj]], [[4wbk|4wbk]]</td></tr> | |||
<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=4tkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tkb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tkb RCSB], [http://www.ebi.ac.uk/pdbsum/4tkb PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hara, T]] | |||
[[Category: Hirose, M]] | |||
[[Category: Inoue, T]] | [[Category: Inoue, T]] | ||
[[Category: Ishida, H]] | [[Category: Ishida, H]] | ||
[[Category: | [[Category: Kakinouchi, K]] | ||
[[Category: Matsuoka, D]] | |||
[[Category: Matsuoka, S]] | |||
[[Category: Mizohata, E]] | [[Category: Mizohata, E]] | ||
[[Category: Murakami, S]] | [[Category: Murakami, S]] | ||
[[Category: | [[Category: Murata, M]] | ||
[[Category: Sugiyama, S]] | [[Category: Sugiyama, S]] | ||
[[Category: | [[Category: Antiparallel beta barrel]] | ||
[[Category: | [[Category: Fatty acid-binding protein]] | ||
[[Category: Human]] | |||
[[Category: Lipid binding protein]] | |||
Revision as of 19:33, 28 January 2015
The 0.86 angstrom X-ray structure of the human heart fatty acid-binding protein complexed with lauric acidThe 0.86 angstrom X-ray structure of the human heart fatty acid-binding protein complexed with lauric acid
Structural highlights
Function[FABPH_HUMAN] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. Publication Abstract from PubMedLong-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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