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New page: left|200px<br /><applet load="2ft9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ft9, resolution 2.50Å" /> '''Crystal structure of... |
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== | ==Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic acid== | ||
The family of the liver bile acid-binding proteins (L-BABPs), formerly | <StructureSection load='2ft9' size='340' side='right'caption='[[2ft9]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ft9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ambystoma_mexicanum Ambystoma mexicanum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FT9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene></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=2ft9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ft9 OCA], [https://pdbe.org/2ft9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ft9 RCSB], [https://www.ebi.ac.uk/pdbsum/2ft9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ft9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FABP2_AMBME FABP2_AMBME] Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity). The specificity of axolotl L-FABP differs from that of LB-FABP. Binds 2 ligands per protein molecule. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ft/2ft9_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ft9 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The family of the liver bile acid-binding proteins (L-BABPs), formerly called liver basic fatty acid-binding proteins (Lb-FABPs) shares fold and sequence similarity with the paralogous liver fatty acid-binding proteins (L-FABPs) but has a different stoichiometry and specificity of ligand binding. This article describes the first X-ray structure of a member of the L-BABP family, axolotl (Ambystoma mexicanum) L-BABP, bound to two different ligands: cholic and oleic acid. The protein binds one molecule of oleic acid in a position that is significantly different from that of either of the two molecules that bind to rat liver FABP. The stoichiometry of binding of cholate is of two ligands per protein molecule, as observed in chicken L-BABP. The cholate molecule that binds buried most deeply into the internal cavity overlaps well with the analogous bound to chicken L-BABP, whereas the second molecule, which interacts with the first only through hydrophobic contacts, is more external and exposed to the solvent. | |||
Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic and oleic acid.,Capaldi S, Guariento M, Perduca M, Di Pietro SM, Santome JA, Monaco HL Proteins. 2006 Jul 1;64(1):79-88. PMID:16555310<ref>PMID:16555310</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 2ft9" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ambystoma mexicanum]] | [[Category: Ambystoma mexicanum]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Capaldi | [[Category: Capaldi S]] | ||
[[Category: | [[Category: Di Pietro SM]] | ||
[[Category: | [[Category: Guariento M]] | ||
[[Category: | [[Category: Monaco HL]] | ||
[[Category: | [[Category: Perduca M]] | ||
[[Category: Santome | [[Category: Santome JA]] | ||
Latest revision as of 11:45, 25 October 2023
Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic acidCrystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic acid
Structural highlights
FunctionFABP2_AMBME Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity). The specificity of axolotl L-FABP differs from that of LB-FABP. Binds 2 ligands per protein molecule. 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 PubMedThe family of the liver bile acid-binding proteins (L-BABPs), formerly called liver basic fatty acid-binding proteins (Lb-FABPs) shares fold and sequence similarity with the paralogous liver fatty acid-binding proteins (L-FABPs) but has a different stoichiometry and specificity of ligand binding. This article describes the first X-ray structure of a member of the L-BABP family, axolotl (Ambystoma mexicanum) L-BABP, bound to two different ligands: cholic and oleic acid. The protein binds one molecule of oleic acid in a position that is significantly different from that of either of the two molecules that bind to rat liver FABP. The stoichiometry of binding of cholate is of two ligands per protein molecule, as observed in chicken L-BABP. The cholate molecule that binds buried most deeply into the internal cavity overlaps well with the analogous bound to chicken L-BABP, whereas the second molecule, which interacts with the first only through hydrophobic contacts, is more external and exposed to the solvent. Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic and oleic acid.,Capaldi S, Guariento M, Perduca M, Di Pietro SM, Santome JA, Monaco HL Proteins. 2006 Jul 1;64(1):79-88. PMID:16555310[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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