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New page: left|200px<br /><applet load="1tah" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tah, resolution 3.0Å" /> '''THE CRYSTAL STRUCTURE...
 
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[[Image:1tah.gif|left|200px]]<br /><applet load="1tah" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1tah, resolution 3.0&Aring;" />
'''THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE'''<br />


==Overview==
==THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE==
The family of lipases (triacylglycerol-acyl-hydrolases EC 3.1.1.3), constitutes an interesting class of enzymes because of their ability to, interact with lipid-water interfaces, their wide range of substrate, specificities, and their potential industrial applications. Here we report, the first crystal structure of a bacterial lipase, from Pseudomonas, glumae. The structure is formed from three domains, the largest of which, contains a subset of the alpha/beta hydrolase fold and a calcium site., Asp263, the acidic residue in the catalytic triad, has previously been, mutated into an alanine with only a modest reduction in activity.
<StructureSection load='1tah' size='340' side='right'caption='[[1tah]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1tah]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_glumae Burkholderia glumae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TAH 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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1tah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tah OCA], [https://pdbe.org/1tah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tah RCSB], [https://www.ebi.ac.uk/pdbsum/1tah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tah ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LIP_BURPL LIP_BURPL] Catalyzes the hydrolysis of triacylglycerol.<ref>PMID:1476423</ref> <ref>PMID:7786905</ref>
== 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/ta/1tah_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=1tah ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The family of lipases (triacylglycerol-acyl-hydrolases EC 3.1.1.3) constitutes an interesting class of enzymes because of their ability to interact with lipid-water interfaces, their wide range of substrate specificities, and their potential industrial applications. Here we report the first crystal structure of a bacterial lipase, from Pseudomonas glumae. The structure is formed from three domains, the largest of which contains a subset of the alpha/beta hydrolase fold and a calcium site. Asp263, the acidic residue in the catalytic triad, has previously been mutated into an alanine with only a modest reduction in activity.


==About this Structure==
The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate.,Noble ME, Cleasby A, Johnson LN, Egmond MR, Frenken LG FEBS Lett. 1993 Sep 27;331(1-2):123-8. PMID:8405390<ref>PMID:8405390</ref>
1TAH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_glumae Burkholderia glumae] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TAH OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate., Noble ME, Cleasby A, Johnson LN, Egmond MR, Frenken LG, FEBS Lett. 1993 Sep 27;331(1-2):123-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8405390 8405390]
</div>
<div class="pdbe-citations 1tah" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Lipase 3D Structures|Lipase 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Burkholderia glumae]]
[[Category: Burkholderia glumae]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Triacylglycerol lipase]]
[[Category: Cleasby A]]
[[Category: Cleasby, A.]]
[[Category: Egmond M]]
[[Category: Egmond, M.]]
[[Category: Frenken LGJ]]
[[Category: Frenken, L.G.J.]]
[[Category: Johnson LN]]
[[Category: Johnson, L.N.]]
[[Category: Noble MEM]]
[[Category: Noble, M.E.M.]]
[[Category: CA]]
[[Category: hydrolase(carboxylic esterase)]]
 
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