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1du4

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(New page: 200px<br /><applet load="1du4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1du4, resolution 2.5&Aring;" /> '''THE STRUCTURAL ORIGIN...)
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[[Image:1du4.jpg|left|200px]]<br /><applet load="1du4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1du4, resolution 2.5&Aring;" />
 
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'''THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE OTHER STRUCTURE DETAILS'''<br />
 
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==Overview==
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==THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE OTHER STRUCTURE DETAILS==
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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='1du4' size='340' side='right'caption='[[1du4]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1du4]] is a 4 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=1DU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DU4 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]] 2.5&#8491;</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=1du4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1du4 OCA], [https://pdbe.org/1du4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1du4 RCSB], [https://www.ebi.ac.uk/pdbsum/1du4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1du4 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/du/1du4_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=1du4 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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1DU4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus]. 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=1DU4 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: alpha-beta protein]]
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[[Category: interfacial activation]]
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[[Category: lipase]]
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[[Category: thermomyces linuginosa]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:35:04 2007''
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Current revision

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

PDB ID 1du4

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