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| | ==Crystal structure of apo Zebrafish Ileal Bile Acid-Binding Protein== | | ==Crystal structure of apo Zebrafish Ileal Bile Acid-Binding Protein== |
| - | <StructureSection load='3elx' size='340' side='right' caption='[[3elx]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='3elx' size='340' side='right'caption='[[3elx]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3elx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ELX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ELX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3elx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ELX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ELX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3elz|3elz]], [[3em0|3em0]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabp6, zgc:92421 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3elx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3elx OCA], [https://pdbe.org/3elx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3elx RCSB], [https://www.ebi.ac.uk/pdbsum/3elx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3elx ProSAT]</span></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=3elx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3elx OCA], [http://pdbe.org/3elx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3elx RCSB], [http://www.ebi.ac.uk/pdbsum/3elx PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6IMW5_DANRE Q6IMW5_DANRE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/el/3elx_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/el/3elx_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | ==See Also== | | ==See Also== |
| - | *[[Fatty acid-binding protein|Fatty acid-binding protein]] | + | *[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Brachidanio rerio]] | + | [[Category: Danio rerio]] |
| - | [[Category: Capaldi, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Fessas, D]] | + | [[Category: Capaldi S]] |
| - | [[Category: Monaco, H L]] | + | [[Category: Fessas D]] |
| - | [[Category: Perduca, M]] | + | [[Category: Monaco HL]] |
| - | [[Category: Saccomani, G]] | + | [[Category: Perduca M]] |
| - | [[Category: Signorelli, M]] | + | [[Category: Saccomani G]] |
| - | [[Category: Cholic acid]]
| + | [[Category: Signorelli M]] |
| - | [[Category: Ileal bile acid-bindign protein]]
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| - | [[Category: Lipid binding protein]]
| + | |
| - | [[Category: Lipid-binding]]
| + | |
| - | [[Category: Transport]]
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| - | [[Category: Zebrafish]]
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| Structural highlights
Function
Q6IMW5_DANRE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The ileal bile acid-binding proteins (I-BABPs), also called ileal lipid-binding proteins or gastrotropins, belong to the family of the fatty acid-binding proteins and play an important role in the solubilization and transport of bile acids in the enterocyte. This article describes the expression, purification, crystallization, and three-dimensional structure determination of zebrafish (Danio rerio) I-BABP both in its apo form and bound to cholic acid. This is the first X-ray structure of an I-BABP. The structure of the apoprotein was determined to a resolution of 1.6 A, and two different monoclinic crystal forms of the holoprotein were solved and refined to 2.2 A resolution. Three protein molecules are present in the asymmetric unit of one of the co-crystal forms and two in the other, and therefore, the results of this study refer to observations made on five different protein molecules in the crystalline state. In every case, two cholate ligands were found bound in approximately the same position in the internal cavity of the protein molecules, but an unexpected result is the presence of clear and unambiguous electron density for several cholate molecules bound on hydrophobic patches on the surface of all the five independent protein molecules examined. Isothermal titration calorimetry was used for the thermodynamic characterization of the binding mechanism and has yielded results that are consistent with the X-ray data. Ligand binding is described in detail, and the conformational changes undergone by the protein molecule in the apo-to-holo transition are examined by superposition of the apo- and holoprotein models. The structure of the holoprotein is also compared with that of the liver BABP from the same species and those of other I-BABPs determined by NMR.
The X-Ray structure of zebrafish (Danio rerio) ileal bile acid-binding protein reveals the presence of binding sites on the surface of the protein molecule.,Capaldi S, Saccomani G, Fessas D, Signorelli M, Perduca M, Monaco HL J Mol Biol. 2009 Jan 9;385(1):99-116. Epub 2008 Oct 14. PMID:18952094[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Capaldi S, Saccomani G, Fessas D, Signorelli M, Perduca M, Monaco HL. The X-Ray structure of zebrafish (Danio rerio) ileal bile acid-binding protein reveals the presence of binding sites on the surface of the protein molecule. J Mol Biol. 2009 Jan 9;385(1):99-116. Epub 2008 Oct 14. PMID:18952094 doi:http://dx.doi.org/S0022-2836(08)01266-7
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