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| | <StructureSection load='4fbm' size='340' side='right'caption='[[4fbm]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='4fbm' size='340' side='right'caption='[[4fbm]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fbm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Miscellaneous_nucleic_acid Miscellaneous nucleic acid]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FBM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FBM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fbm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FBM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fbl|4fbl]]</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=4fbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fbm OCA], [https://pdbe.org/4fbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fbm RCSB], [https://www.ebi.ac.uk/pdbsum/4fbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fbm 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=4fbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fbm OCA], [http://pdbe.org/4fbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fbm RCSB], [http://www.ebi.ac.uk/pdbsum/4fbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fbm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Miscellaneous nucleic acid]] | + | [[Category: Unidentified]] |
| - | [[Category: Antonia, Y Dall]] | + | [[Category: Bongen P]] |
| - | [[Category: Bongen, P]] | + | [[Category: Bornscheuer U]] |
| - | [[Category: Bornscheuer, U]] | + | [[Category: Chow J]] |
| - | [[Category: Chow, J]] | + | [[Category: Dall Antonia Y]] |
| - | [[Category: Eckstein, M]] | + | [[Category: Eckstein M]] |
| - | [[Category: Fersini, F]] | + | [[Category: Fersini F]] |
| - | [[Category: Jaeger, K E]] | + | [[Category: Jaeger K-E]] |
| - | [[Category: Kovavic, F]] | + | [[Category: Kovavic F]] |
| - | [[Category: Krauss, U]] | + | [[Category: Krauss U]] |
| - | [[Category: Lauinger, B]] | + | [[Category: Lauinger B]] |
| - | [[Category: Liese, A]] | + | [[Category: Liese A]] |
| - | [[Category: Menyes, I]] | + | [[Category: Menyes I]] |
| - | [[Category: Mueller-Dieckmann, J]] | + | [[Category: Mueller-Dieckmann J]] |
| - | [[Category: Pietruszka, J]] | + | [[Category: Pietruszka J]] |
| - | [[Category: SPINE, Structural Proteomics in Europe]]
| + | [[Category: Schmeisser C]] |
| - | [[Category: Schmeisser, C]] | + | [[Category: Schmidt M]] |
| - | [[Category: Schmidt, M]] | + | [[Category: Streit WR]] |
| - | [[Category: Streit, W R]] | + | [[Category: Thum O]] |
| - | [[Category: Thum, O]] | + | |
| - | [[Category: Alpha/beta hydrolase]]
| + | |
| - | [[Category: Enzyme function initiative]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lipase]]
| + | |
| - | [[Category: Spine]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structural proteomics in europe]]
| + | |
| - | [[Category: Thermostable]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Triacylglycerol lipases (EC 3.1.1.3) catalyze both hydrolysis and synthesis reactions with a broad spectrum of substrates rendering them especially suitable for many biotechnological applications. Most lipases used today originate from mesophilic organisms and are susceptible to thermal denaturation whereas only few possess high thermotolerance. Here, we report on the identification and characterization of two novel thermostable bacterial lipases identified by functional metagenomic screenings. Metagenomic libraries were constructed from enrichment cultures maintained at 65 to 75 degrees C and screened resulting in the identification of initially 10 clones with lipolytic activities. Subsequently, two ORFs were identified encoding lipases, LipS and LipT. Comparative sequence analyses suggested that both enzymes are members of novel lipase families. LipS is a 30.2 kDa protein and revealed a half-life of 48 h at 70 degrees C. The lipT gene encoded for a multimeric enzyme with a half-life of 3 h at 70 degrees C. LipS had an optimum temperature at 70 degrees C and LipT at 75 degrees C. Both enzymes catalyzed hydrolysis of long-chain (C(12) and C(14)) fatty acid esters and additionally hydrolyzed a number of industry-relevant substrates. LipS was highly specific for (R)-ibuprofen-phenyl ester with an enantiomeric excess (ee) of 99%. Furthermore, LipS was able to synthesize 1-propyl laurate and 1-tetradecyl myristate at 70 degrees C with rates similar to those of the lipase CalB from Candida antarctica. LipS represents the first example of a thermostable metagenome-derived lipase with significant synthesis activities. Its X-ray structure was solved with a resolution of 1.99 A revealing an unusually compact lid structure.
The Metagenome-Derived Enzymes LipS and LipT Increase the Diversity of Known Lipases.,Chow J, Kovacic F, Dall Antonia Y, Krauss U, Fersini F, Schmeisser C, Lauinger B, Bongen P, Pietruszka J, Schmidt M, Menyes I, Bornscheuer UT, Eckstein M, Thum O, Liese A, Mueller-Dieckmann J, Jaeger KE, Streit WR PLoS One. 2012;7(10):e47665. doi: 10.1371/journal.pone.0047665. Epub 2012 Oct 24. PMID:23112831[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chow J, Kovacic F, Dall Antonia Y, Krauss U, Fersini F, Schmeisser C, Lauinger B, Bongen P, Pietruszka J, Schmidt M, Menyes I, Bornscheuer UT, Eckstein M, Thum O, Liese A, Mueller-Dieckmann J, Jaeger KE, Streit WR. The Metagenome-Derived Enzymes LipS and LipT Increase the Diversity of Known Lipases. PLoS One. 2012;7(10):e47665. doi: 10.1371/journal.pone.0047665. Epub 2012 Oct 24. PMID:23112831 doi:http://dx.doi.org/10.1371/journal.pone.0047665
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