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| | <StructureSection load='1gt6' size='340' side='right'caption='[[1gt6]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1gt6' size='340' side='right'caption='[[1gt6]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gt6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_632.91 Cbs 632.91]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GT6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gt6]] is a 2 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=1GT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GT6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dt3|1dt3]], [[1dt5|1dt5]], [[1dte|1dte]], [[1du4|1du4]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5541 CBS 632.91])</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=1gt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gt6 OCA], [https://pdbe.org/1gt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gt6 RCSB], [https://www.ebi.ac.uk/pdbsum/1gt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gt6 ProSAT]</span></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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gt6 OCA], [http://pdbe.org/1gt6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gt6 RCSB], [http://www.ebi.ac.uk/pdbsum/1gt6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gt6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LIP_THELA LIP_THELA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Lipase|Lipase]] | + | *[[Lipase 3D Structures|Lipase 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cbs 632 91]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Triacylglycerol lipase]] | + | [[Category: Thermomyces lanuginosus]] |
| - | [[Category: Brzozowski, A M]] | + | [[Category: Brzozowski AM]] |
| - | [[Category: Ivanova, M G]] | + | [[Category: Ivanova MG]] |
| - | [[Category: Patkar, S A]] | + | [[Category: Patkar SA]] |
| - | [[Category: Svendsen, A]] | + | [[Category: Svendsen A]] |
| - | [[Category: Verger, R]] | + | [[Category: Verger R]] |
| - | [[Category: Vind, J]] | + | [[Category: Vind J]] |
| - | [[Category: Yapoudjian, S]] | + | [[Category: Yapoudjian S]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lipase]]
| + | |
| - | [[Category: Lipid degradation]]
| + | |
| - | [[Category: Zymogen]]
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| Structural highlights
Function
LIP_THELA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The binding of Thermomyces lanuginosa lipase and its mutants [TLL(S146A), TLL(W89L), TLL(W117F, W221H, W260H)] to the mixed micelles of cis-parinaric acid/sodium taurodeoxycholate at pH 5.0 led to the quenching of the intrinsic tryptophan fluorescence emission (300-380 nm) and to a simultaneous increase in the cis-parinaric acid fluorescence emission (380-500 nm). These findings were used to characterize the Thermomyces lanuginosa lipase/cis-parinaric acid interactions occurring in the presence of sodium taurodeoxycholate.The fluorescence resonance energy transfer and Stern-Volmer quenching constant values obtained were correlated with the accessibility of the tryptophan residues to the cis-parinaric acid and with the lid opening ability of Thermomyces lanuginosa lipase (and its mutants). TLL(S146A) was found to have the highest fluorescence resonance energy transfer. In addition, a TLL(S146A)/oleic acid complex was crystallised and its three-dimensional structure was solved. Surprisingly, two possible binding modes (sn-1 and antisn1) were found to exist between oleic acid and the catalytic cleft of the open conformation of TLL(S146A). Both binding modes involved an interaction with tryptophan 89 of the lipase lid, in agreement with fluorescence resonance energy transfer experiments.As a consequence, we concluded that TLL(S146A) mutant is not an appropriate substitute for the wild-type Thermomyces lanuginosa lipase for mimicking the interaction between the wild-type enzyme and lipids.
Binding of Thermomyces (Humicola) lanuginosa lipase to the mixed micelles of cis-parinaric acid/NaTDC.,Yapoudjian S, Ivanova MG, Brzozowski AM, Patkar SA, Vind J, Svendsen A, Verger R Eur J Biochem. 2002 Mar;269(6):1613-21. PMID:11895431[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yapoudjian S, Ivanova MG, Brzozowski AM, Patkar SA, Vind J, Svendsen A, Verger R. Binding of Thermomyces (Humicola) lanuginosa lipase to the mixed micelles of cis-parinaric acid/NaTDC. Eur J Biochem. 2002 Mar;269(6):1613-21. PMID:11895431
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