6mk2
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Coleus blumei rosmarinic acid synthase (RAS) in complex with 4-coumaroyl-(R)-3-(4-hydroxyphenyl)lactate== | |
| + | <StructureSection load='6mk2' size='340' side='right'caption='[[6mk2]], [[Resolution|resolution]] 3.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6mk2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Coleus Coleus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MK2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MK2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JUV:(2R)-3-(4-hydroxyphenyl)-2-{[(2E)-3-(4-hydroxyphenyl)prop-2-enoyl]oxy}propanoic+acid'>JUV</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4142 Coleus])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Rosmarinate_synthase Rosmarinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.140 2.3.1.140] </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=6mk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mk2 OCA], [http://pdbe.org/6mk2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mk2 RCSB], [http://www.ebi.ac.uk/pdbsum/6mk2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mk2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/RAS_PLESU RAS_PLESU]] Involved in the biosynthesis of rosmarinic acid, a compound with antiviral, antimicrobial and anti-inflammatory activities. Can use 4-coumaroyl- and caffeoyl-CoA as hydroxycinnamoyl donors and 4-Hydroxyphenyllactate and 3.4-Dihydroxyphenyllactate, but not shikimate or quinate, as hydroxycinnamoyl acceptors. Can also putatively catalyze amide formation with D-amino acids as acceptors.<ref>PMID:17047986</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | As a means to maintain their sessile lifestyle amid challenging environments, plants produce an enormous diversity of compounds as chemical defenses against biotic and abiotic insults. The underpinning metabolic pathways that support the biosynthesis of these specialized chemicals in divergent plant species provide a rich arena for understanding the molecular evolution of complex metabolic traits. Rosmarinic acid (RA) is a phenolic natural product first discovered in plants of the mint family (Lamiaceae) and is recognized for its wide range of medicinal properties and potential applications in human dietary and medical interventions. Interestingly, the RA chemotype is present sporadically in multiple taxa of flowering plants as well as some hornworts and ferns, prompting the question whether its biosynthesis arose independently across different lineages. Here we report the elucidation of the RA biosynthetic pathway in Phacelia campanularia (desert bells). This species represents the borage family (Boraginaceae), an RA-producing family closely related to the Lamiaceae within the Lamiids clade. Using a multi-omics approach in combination with functional characterization of candidate genes both in vitro and in vivo, we found that RA biosynthesis in P. campanularia involves specific activities of a BAHD acyltransferase and two cytochrome P450 hydroxylases. Further phylogenetic and comparative structure-function analyses of the P. campanularia RA biosynthetic enzymes clearly indicate that RA biosynthesis has evolved independently at least twice in the Lamiids, an exemplary case of chemotypic convergence through disparate evolutionary trajectories. | ||
| - | + | Independent evolution of rosmarinic acid biosynthesis in two sister families under the Lamiids clade of flowering plants.,Levsh O, Pluskal T, Carballo V, Mitchell AJ, Weng JK J Biol Chem. 2019 Oct 18;294(42):15193-15205. doi: 10.1074/jbc.RA119.010454. Epub, 2019 Sep 3. PMID:31481469<ref>PMID:31481469</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6mk2" style="background-color:#fffaf0;"></div> |
| - | [[Category: Levsh, O | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Coleus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rosmarinate synthase]] | ||
| + | [[Category: Levsh, O L]] | ||
| + | [[Category: Weng, J K]] | ||
| + | [[Category: Bahd acyltransferase]] | ||
| + | [[Category: Hydroxycinnamoyltransferase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 09:34, 30 October 2019
Crystal structure of Coleus blumei rosmarinic acid synthase (RAS) in complex with 4-coumaroyl-(R)-3-(4-hydroxyphenyl)lactate
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