5tgl

<table><tr><td colspan='2'>[[5tgl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_16457 Atcc 16457]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TGL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TGL FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEE:N-HEXYLPHOSPHONATE+ETHYL+ESTER'>HEE</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5tgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tgl OCA], [http://pdbe.org/5tgl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tgl RCSB], [http://www.ebi.ac.uk/pdbsum/5tgl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tgl ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Lipases are hydrolytic enzymes which break down triacylglycerides into free fatty acids and glycerols. They have been classified as serine hydrolases owing to their inhibition by diethyl p-nitrophenyl phosphate. Lipase activity is greatly increased at the lipid-water interface, a phenomenon known as interfacial activation. X-ray analysis has revealed the atomic structures of two triacylglycerol lipases, unrelated in sequence: the human pancreatic lipase (hPL)4, and an enzyme isolated from the fungus Rhizomucor (formerly Mucor) miehei (RmL). In both enzymes the active centres contain structurally analogous Asp-His-Ser triads (characteristic of serine proteinases), which are buried completely beneath a short helical segment, or 'lid'. Here we present the crystal structure (at 3 A resolution) of a complex of R. miehei lipase with n-hexylphosphonate ethyl ester in which the enzyme's active site is exposed by the movement of the helical lid. This movement also increases the nonpolarity of the surface surrounding the catalytic site. We propose that the structure of the enzyme in this complex is equivalent to the activated state generated by the oil-water interface.

A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex.,Brzozowski AM, Derewenda U, Derewenda ZS, Dodson GG, Lawson DM, Turkenburg JP, Bjorkling F, Huge-Jensen B, Patkar SA, Thim L Nature. 1991 Jun 6;351(6326):491-4. PMID:2046751<ref>PMID:2046751</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 5tgl" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 16457]]

[[Category: Triacylglycerol lipase]]

[[Category: Bjorkling, F]]

[[Category: Brzozowski, A M]]

[[Category: Derewenda, U]]

[[Category: Derewenda, Z S]]

[[Category: Dodson, G G]]

[[Category: Huge-Jensen, B]]

[[Category: Lawson, D]]

[[Category: Patkar, S R]]

[[Category: Thim, L]]

[[Category: Turkenburg, J P]]