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| | <StructureSection load='6cl4' size='340' side='right'caption='[[6cl4]], [[Resolution|resolution]] 2.64Å' scene=''> | | <StructureSection load='6cl4' size='340' side='right'caption='[[6cl4]], [[Resolution|resolution]] 2.64Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6cl4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Uncultivated_bacterium Uncultivated bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CL4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CL4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cl4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CL4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CL4 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lipc12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=77133 uncultivated bacterium])</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]] 2.64Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=6cl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cl4 OCA], [https://pdbe.org/6cl4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cl4 RCSB], [https://www.ebi.ac.uk/pdbsum/6cl4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cl4 ProSAT]</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=6cl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cl4 OCA], [http://pdbe.org/6cl4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cl4 RCSB], [http://www.ebi.ac.uk/pdbsum/6cl4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cl4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G1APT8_9BACT G1APT8_9BACT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6cl4" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6cl4" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Lipase 3D Structures|Lipase 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Triacylglycerol lipase]] | + | [[Category: Uncultured bacterium]] |
| - | [[Category: Uncultivated bacterium]]
| + | [[Category: Glogauer A]] |
| - | [[Category: Glogauer, A]] | + | [[Category: Iulek J]] |
| - | [[Category: Iulek, J]] | + | [[Category: Krieger N]] |
| - | [[Category: Krieger, N]] | + | [[Category: Martini VP]] |
| - | [[Category: Martini, V P]] | + | [[Category: Souza EM]] |
| - | [[Category: Souza, E M]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lipase]]
| + | |
| Structural highlights
Function
G1APT8_9BACT
Publication Abstract from PubMed
Metagenomics is a modern approach to discovery of new enzymes with novel properties. This article reports the structure of a new lipase, belonging to family I.1, obtained by means of metagenomics. Its structure presents a fold typical of alpha/beta hydrolases, with the lid in closed conformation. The protein was previously shown to present high thermostability and to be stable in aqueous solutions of polar organic solvents at high concentrations [30% (V/V)]. Molecular dynamics studies showed that the protein maintains its structure well in organic solvents. They also suggested that its thermostability might be enhanced if it were mutated to present a disulfide bond similar to that typically found in lipase family I.2. These findings identify this lipase as a good candidate for further improvement through protein engineering.
Structure solution and analyses of the first true lipase obtained from metagenomics indicate potential for increased thermostability.,Martini VP, Krieger N, Glogauer A, Souza EM, Iulek J N Biotechnol. 2019 Jul 12;53:65-72. doi: 10.1016/j.nbt.2019.07.001. PMID:31306784[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Martini VP, Krieger N, Glogauer A, Souza EM, Iulek J. Structure solution and analyses of the first true lipase obtained from metagenomics indicate potential for increased thermostability. N Biotechnol. 2019 Jul 12;53:65-72. doi: 10.1016/j.nbt.2019.07.001. PMID:31306784 doi:http://dx.doi.org/10.1016/j.nbt.2019.07.001
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