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1lpp

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ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lpp"

Categories: Diutina rugosa | Large Structures | Cygler MC | Grochulski PG

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-[[Image:1lpp.jpg|left|200px]]<br /><applet load="1lpp" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1lpp, resolution 2.18&Aring;" />
-'''ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE'''<br />
-==Overview==
+==ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE==
-The structures of Candida rugosa lipase-inhibitor complexes demonstrate, that the scissile fatty acyl chain is bound in a narrow, hydrophobic, tunnel which is unique among lipases studied to date. Modeling of, triglyceride binding suggests that the bound lipid must adopt a "tuning, fork" conformation. The complexes, analogs of tetrahedral intermediates of, the acylation and deacylation steps of the reaction pathway, localize the, components of the oxyanion hole and define the stereochemistry of ester, hydrolysis. Comparison with other lipases suggests that the positioning of, the scissile fatty acyl chain and ester bond and the stereochemistry of, hydrolysis are the same in all lipases which share the, alpha/beta-hydrolase fold.
+<StructureSection load='1lpp' size='340' side='right'caption='[[1lpp]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1lpp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Diutina_rugosa Diutina rugosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LPP 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]] 2.18&#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>, <scene name='pdbligand=HDS:1-HEXADECANOSULFONIC+ACID'>HDS</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1lpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lpp OCA], [https://pdbe.org/1lpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lpp RCSB], [https://www.ebi.ac.uk/pdbsum/1lpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lpp ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LIP1_DIURU LIP1_DIURU]
+== 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/lp/1lpp_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=1lpp ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-LPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NAG, CA and HDS as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1LPP OCA].
+*[[Lipase 3D Structures|Lipase 3D Structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase., Grochulski P, Bouthillier F, Kazlauskas RJ, Serreqi AN, Schrag JD, Ziomek E, Cygler M, Biochemistry. 1994 Mar 29;33(12):3494-500. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8142346 8142346]
+[[Category: Diutina rugosa]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Triacylglycerol lipase]]
+[[Category: Cygler MC]]
-[[Category: Cygler, M.C.]]
+[[Category: Grochulski PG]]
-[[Category: Grochulski, P.G.]]
-[[Category: CA]]
-[[Category: HDS]]
-[[Category: NAG]]
-[[Category: hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:46:05 2007''

1lpp

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ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE

Structural highlights

Function

Evolutionary Conservation

See Also

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