6cl4: Difference between revisions
New page: '''Unreleased structure''' The entry 6cl4 is ON HOLD Authors: Iulek, J., Martini, V.P., Krieger, N., Glogauer, A., Souza, E.M. Description: LipC12 -Lipase from metagenomics [[Category:... |
No edit summary |
||
| (4 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==LipC12 - Lipase from metagenomics== | |||
<StructureSection load='6cl4' size='340' side='right'caption='[[6cl4]], [[Resolution|resolution]] 2.64Å' scene=''> | |||
== Structural highlights == | |||
<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='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='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> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/G1APT8_9BACT G1APT8_9BACT] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:31306784</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6cl4" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Iulek | ==See Also== | ||
[[Category: Krieger | *[[Lipase 3D Structures|Lipase 3D Structures]] | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Uncultured bacterium]] | |||
[[Category: Glogauer A]] | |||
[[Category: Iulek J]] | |||
[[Category: Krieger N]] | |||
[[Category: Martini VP]] | |||
[[Category: Souza EM]] | |||
Latest revision as of 18:06, 4 October 2023
LipC12 - Lipase from metagenomicsLipC12 - Lipase from metagenomics
Structural highlights
FunctionPublication Abstract from PubMedMetagenomics 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 AlsoReferences
|
| ||||||||||||||||