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[[Image:1aql.png|left|200px]]


{{STRUCTURE_1aql| PDB=1aql | SCENE= }}
==CRYSTAL STRUCTURE OF BOVINE BILE-SALT ACTIVATED LIPASE COMPLEXED WITH TAUROCHOLATE==
<StructureSection load='1aql' size='340' side='right'caption='[[1aql]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1aql]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AQL 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TCH:TAUROCHOLIC+ACID'>TCH</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=1aql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aql OCA], [https://pdbe.org/1aql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aql RCSB], [https://www.ebi.ac.uk/pdbsum/1aql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aql ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CEL_BOVIN CEL_BOVIN] Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.
== 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/aq/1aql_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1aql ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: The intestinally located pancreatic enzyme, bile salt activated lipase (BAL), possesses unique activities for digesting different kinds of lipids. It also differs from other lipases in a requirement of bile salts for activity. A structure-based explanation for these unique properties has not been reached so far due to the absence of a three-dimensional structure. RESULTS: The crystal structures of bovine BAL and its complex with taurocholate have been determined at 2.8 A resolution. The overall structure of BAL belongs to the alpha/beta hydrolase fold family. Two bile salt binding sites were found in each BAL molecule within the BAL-taurocholate complex structure. One of these sites is located close to a hairpin loop near the active site. Upon the binding of taurocholate, this loop becomes less mobile and assumes a different conformation. The other bile salt binding site is located remote from the active site. In both structures, BAL forms similar dimers with the active sites facing each other. CONCLUSIONS: Bile salts activate BAL by binding to a relatively short ten-residue loop near the active site, and stabilize the loop in an open conformation. Presumably, this conformational change leads to the formation of the substrate-binding site, as suggested from kinetic data. The BAL dimer observed in the crystal structure may also play a functional role under physiological conditions.


===CRYSTAL STRUCTURE OF BOVINE BILE-SALT ACTIVATED LIPASE COMPLEXED WITH TAUROCHOLATE===
The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism.,Wang X, Wang CS, Tang J, Dyda F, Zhang XC Structure. 1997 Sep 15;5(9):1209-18. PMID:9331420<ref>PMID:9331420</ref>


{{ABSTRACT_PUBMED_9331420}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 1aql" style="background-color:#fffaf0;"></div>
[[1aql]] is a 2 chain structure of [[Lipase]] with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQL OCA].


==See Also==
==See Also==
*[[Lipase|Lipase]]
*[[Cholesterol esterase 3D structures|Cholesterol esterase 3D structures]]
 
*[[Lipase 3D Structures|Lipase 3D Structures]]
==Reference==
== References ==
<ref group="xtra">PMID:009331420</ref><references group="xtra"/>
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Sterol esterase]]
[[Category: Large Structures]]
[[Category: Wang, X.]]
[[Category: Wang X]]
[[Category: Zhang, X.]]
[[Category: Zhang X]]
[[Category: Glycoprotein]]
[[Category: Hydrolase]]
[[Category: Lipid degradation]]
[[Category: Serine esterase]]
Retrieved from "https://proteopedia.org/1aql"