5e4d: Difference between revisions
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<table><tr><td colspan='2'>[[5e4d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Davallia_tyermanii Davallia tyermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E4D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E4D FirstGlance]. <br> | <table><tr><td colspan='2'>[[5e4d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Davallia_tyermanii Davallia tyermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E4D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E4D FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e46|5e46]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5e46|5e46]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5e4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4d OCA], [http://pdbe.org/5e4d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e4d RCSB], [http://www.ebi.ac.uk/pdbsum/5e4d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4d ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5e4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4d OCA], [http://pdbe.org/5e4d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e4d RCSB], [http://www.ebi.ac.uk/pdbsum/5e4d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Homology and similarity based approaches are most widely used for the identification of new enzymes for biocatalysis. However, they are not suitable to find truly novel scaffolds with a desired function and this averts options and diversity. Hydroxynitrile lyases (HNLs) are an example of non-homologous isofunctional enzymes for the synthesis of chiral cyanohydrins. Due to their convergent evolution, finding new representatives is challenging. Here we show the discovery of unique HNL enzymes from the fern Davallia tyermannii by coalescence of transcriptomics, proteomics and enzymatic screening. It is the first protein with a Bet v1-like protein fold exhibiting HNL activity, and has a new catalytic center, as shown by protein crystallography. Biochemical properties of D. tyermannii HNLs open perspectives for the development of a complementary class of biocatalysts for the stereoselective synthesis of cyanohydrins. This work shows that systematic integration of -omics data facilitates discovery of enzymes with unpredictable sequences and helps to extend our knowledge about enzyme diversity. | |||
Enzyme discovery beyond homology: a unique hydroxynitrile lyase in the Bet v1 superfamily.,Lanfranchi E, Pavkov-Keller T, Koehler EM, Diepold M, Steiner K, Darnhofer B, Hartler J, Van Den Bergh T, Joosten HJ, Gruber-Khadjawi M, Thallinger GG, Birner-Gruenberger R, Gruber K, Winkler M, Glieder A Sci Rep. 2017 May 3;7:46738. doi: 10.1038/srep46738. PMID:28466867<ref>PMID:28466867</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5e4d" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:44, 24 December 2020
Hydroxynitrile lyase from the fern Davallia tyermanii in complex with benzoic acidHydroxynitrile lyase from the fern Davallia tyermanii in complex with benzoic acid
Structural highlights
Publication Abstract from PubMedHomology and similarity based approaches are most widely used for the identification of new enzymes for biocatalysis. However, they are not suitable to find truly novel scaffolds with a desired function and this averts options and diversity. Hydroxynitrile lyases (HNLs) are an example of non-homologous isofunctional enzymes for the synthesis of chiral cyanohydrins. Due to their convergent evolution, finding new representatives is challenging. Here we show the discovery of unique HNL enzymes from the fern Davallia tyermannii by coalescence of transcriptomics, proteomics and enzymatic screening. It is the first protein with a Bet v1-like protein fold exhibiting HNL activity, and has a new catalytic center, as shown by protein crystallography. Biochemical properties of D. tyermannii HNLs open perspectives for the development of a complementary class of biocatalysts for the stereoselective synthesis of cyanohydrins. This work shows that systematic integration of -omics data facilitates discovery of enzymes with unpredictable sequences and helps to extend our knowledge about enzyme diversity. Enzyme discovery beyond homology: a unique hydroxynitrile lyase in the Bet v1 superfamily.,Lanfranchi E, Pavkov-Keller T, Koehler EM, Diepold M, Steiner K, Darnhofer B, Hartler J, Van Den Bergh T, Joosten HJ, Gruber-Khadjawi M, Thallinger GG, Birner-Gruenberger R, Gruber K, Winkler M, Glieder A Sci Rep. 2017 May 3;7:46738. doi: 10.1038/srep46738. PMID:28466867[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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