2w22: Difference between revisions
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<StructureSection load='2w22' size='340' side='right' caption='[[2w22]], [[Resolution|resolution]] 2.20Å' scene=''> | ==Activation Mechanism of Bacterial Thermoalkalophilic Lipases== | ||
<StructureSection load='2w22' size='340' side='right'caption='[[2w22]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2w22]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2w22]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_thermocatenulatus Geobacillus thermocatenulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W22 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EGC:2-(2-{2-[2-(2-{2-[2-(2-{2-[4-(1,1,3,3-TETRAMETHYL-BUTYL)-PHENOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>EGC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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=EGC:2-(2-{2-[2-(2-{2-[2-(2-{2-[4-(1,1,3,3-TETRAMETHYL-BUTYL)-PHENOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>EGC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2w22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w22 OCA], [https://pdbe.org/2w22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w22 RCSB], [https://www.ebi.ac.uk/pdbsum/2w22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w22 ProSAT]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q59260_9BACI Q59260_9BACI] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w2/2w22_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w2/2w22_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=2w22 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 25: | Line 28: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2w22" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Lipase|Lipase]] | *[[Lipase 3D Structures|Lipase 3D Structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 33: | Line 37: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Geobacillus thermocatenulatus]] | [[Category: Geobacillus thermocatenulatus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Carrasco-Lopez | [[Category: Carrasco-Lopez C]] | ||
[[Category: Fernandez-Lafuente | [[Category: De Las Rivas B]] | ||
[[Category: Fernandez-Lorente | [[Category: Fernandez-Lafuente R]] | ||
[[Category: Godoy | [[Category: Fernandez-Lorente G]] | ||
[[Category: Guisan | [[Category: Godoy C]] | ||
[[Category: Hermoso | [[Category: Guisan JM]] | ||
[[Category: Palomo | [[Category: Hermoso JA]] | ||
[[Category: Palomo JM]] | |||
Latest revision as of 18:40, 13 December 2023
Activation Mechanism of Bacterial Thermoalkalophilic LipasesActivation Mechanism of Bacterial Thermoalkalophilic Lipases
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe bacterial thermoalkalophilic lipases that hydrolyze saturated fatty acids at 60-75 degrees C and pH 8-10, are grouped as the lipase family I.5. We report here the crystal structure of the lipase from Geobacillus thermocatenulatus, the first structure of a member of the lipase family I.5 showing an open configuration. Unexpectedly, enzyme activation involves large structural rearrangements of around 70 amino acids and the concerted movement of two lids, the 6 and 7 helices, unmasking the active site. Central in the restructuring process of the lids are both the transfer of bulky hydrophobic residues out of the N-terminal end of the 6 helix, and the incorporation of short side chain residues to the 6 C-terminal end. All these structural changes are stabilized by the Zn++ binding domain, which is characteristic of this family of lipases. Two detergent molecules are placed in the active site, mimicking chains of the triglyceride substrate, demonstrating the position of the oxyanion hole and the three pockets that accommodate the sn-1, sn-2 and sn-3 fatty acids chains. The combination of structural and biochemical studies indicate that the lids opening is not mediated by temperature but triggered by interaction with lipid substrate. Activation of bacterial thermoalkalophilic lipases is spurred by dramatic structural rearrangements.,Carrasco-Lopez C, Godoy C, de Las Rivas B, Fernandez-Lorente G, Palomo JM, Guisan JM, Fernandez-Lafuente R, Martinez-Ripoll M, Hermoso JA J Biol Chem. 2008 Dec 3. PMID:19056729[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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