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1ein

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[[Image:1ein.gif|left|200px]]<br /><applet load="1ein" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ein, resolution 3.0&Aring;" />
 
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'''THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE'''<br />
 
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==Overview==
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==THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE==
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The already known X-ray structures of lipases provide little evidence about initial, discrete structural steps occurring in the first phases of their activation in the presence of lipids (process referred to as interfacial activation). To address this problem, five new Thermomyces (formerly Humicola) lanuginosa lipase (TlL) crystal structures have been solved and compared with four previously reported structures of this enzyme. The bias coming from different crystallization media has been minimized by the growth of all crystals under the same crystallization conditions, in the presence of detergent/lipid analogues, with low or high ionic strength as the only main variable. Resulting structures and their characteristic features allowed the identification of three structurally distinct species of this enzyme: low activity form (LA), activated form (A), and fully Active (FA) form. The isomerization of the Cys268-Cys22 disulfide, synchronized with the formation of a new, short alpha(0) helix and flipping of the Arg84 (Arginine switch) located in the lid's proximal hinge, have been postulated as the key, structural factors of the initial transitions between LA and A forms. The experimental results were supplemented by theoretical calculations. The magnitude of the activation barrier between LA (ground state) and A (end state) forms of TlL (10.6 kcal/mol) is comparable to the enthalpic barriers typical for ring flips and disulfide isomerizations at ambient temperatures. This suggests that the sequence of the structural changes, as exemplified in various TlL crystal structures, mirror those that may occur during interfacial activation.
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<StructureSection load='1ein' size='340' side='right'caption='[[1ein]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ein]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EIN FirstGlance]. <br>
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLC:DIUNDECYL+PHOSPHATIDYL+CHOLINE'>PLC</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ein FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ein OCA], [https://pdbe.org/1ein PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ein RCSB], [https://www.ebi.ac.uk/pdbsum/1ein PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ein ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIP_THELA LIP_THELA]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ei/1ein_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ein ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1EIN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus] with <scene name='pdbligand=PLC:'>PLC</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1EIN OCA].
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase., Brzozowski AM, Savage H, Verma CS, Turkenburg JP, Lawson DM, Svendsen A, Patkar S, Biochemistry. 2000 Dec 12;39(49):15071-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11106485 11106485]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Thermomyces lanuginosus]]
[[Category: Thermomyces lanuginosus]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Brozozowski AM]]
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[[Category: Brozozowski, A M.]]
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[[Category: Savage H]]
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[[Category: Savage, H.]]
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[[Category: PLC]]
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[[Category: alpha-beta structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:07 2008''
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Current revision

THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE

PDB ID 1ein

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