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| | <StructureSection load='4r1t' size='340' side='right'caption='[[4r1t]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='4r1t' size='340' side='right'caption='[[4r1t]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4r1t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pethy Pethy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R1T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R1T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4r1t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Petunia_x_hybrida Petunia x hybrida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R1T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=I2I:MOLECULAR+IODINE'>I2I</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I2I:MOLECULAR+IODINE'>I2I</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r1s|4r1s]], [[4r1u|4r1u]]</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=4r1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r1t OCA], [https://pdbe.org/4r1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r1t RCSB], [https://www.ebi.ac.uk/pdbsum/4r1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r1t ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PhCCR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4102 PETHY])</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=4r1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r1t OCA], [http://pdbe.org/4r1t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r1t RCSB], [http://www.ebi.ac.uk/pdbsum/4r1t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r1t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CCR1_PETHY CCR1_PETHY] Involved in the latter stages of lignin biosynthesis (PubMed:24985707). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:25217505, PubMed:24985707). Mediates the conversion of feruloyl CoA to coniferylaldehyde (PubMed:25217505, PubMed:24985707). Also active toward p-coumaroyl-CoA and sinapoyl-CoA (PubMed:25217505, PubMed:24985707). Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (PubMed:24985707).<ref>PMID:24985707</ref> <ref>PMID:25217505</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pethy]] | + | [[Category: Petunia x hybrida]] |
| - | [[Category: Bomati, E K]] | + | [[Category: Bomati EK]] |
| - | [[Category: Bowman, M E]] | + | [[Category: Bowman ME]] |
| - | [[Category: Louie, G V]] | + | [[Category: Louie GV]] |
| - | [[Category: Noel, J P]] | + | [[Category: Noel JP]] |
| - | [[Category: Cinnamoyl-coa reductase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Short-chain dehydrogenase/reductase]]
| + | |
| Structural highlights
Function
CCR1_PETHY Involved in the latter stages of lignin biosynthesis (PubMed:24985707). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:25217505, PubMed:24985707). Mediates the conversion of feruloyl CoA to coniferylaldehyde (PubMed:25217505, PubMed:24985707). Also active toward p-coumaroyl-CoA and sinapoyl-CoA (PubMed:25217505, PubMed:24985707). Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (PubMed:24985707).[1] [2]
Publication Abstract from PubMed
The enzymes cinnamoyl-CoA reductase (CCR) and cinnamyl alcohol dehydrogenase (CAD) catalyze the two key reduction reactions in the conversion of cinnamic acid derivatives into monolignol building blocks for lignin polymers in plant cell walls. Here, we describe detailed functional and structural analyses of CCRs from Medicago truncatula and Petunia hybrida and of an atypical CAD (CAD2) from M. truncatula. These enzymes are closely related members of the short-chain dehydrogenase/reductase (SDR) superfamily. Our structural studies support a reaction mechanism involving a canonical SDR catalytic triad in both CCR and CAD2 and an important role for an auxiliary cysteine unique to CCR. Site-directed mutants of CAD2 (Phe226Ala and Tyr136Phe) that enlarge the phenolic binding site result in a 4- to 10-fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2. This finding demonstrates the potential exploitation of rationally engineered forms of CCR and CAD2 for the targeted modification of monolignol composition in transgenic plants. Thermal denaturation measurements and structural comparisons of various liganded and unliganded forms of CCR and CAD2 highlight substantial conformational flexibility of these SDR enzymes, which plays an important role in the establishment of catalytically productive complexes of the enzymes with their NADPH and phenolic substrates.
Structural Studies of Cinnamoyl-CoA Reductase and Cinnamyl-Alcohol Dehydrogenase, Key Enzymes of Monolignol Biosynthesis.,Pan H, Zhou R, Louie GV, Muhlemann JK, Bomati EK, Bowman ME, Dudareva N, Dixon RA, Noel JP, Wang X Plant Cell. 2014 Sep 12. pii: tpc.114.127399. PMID:25217505[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Muhlemann JK, Woodworth BD, Morgan JA, Dudareva N. The monolignol pathway contributes to the biosynthesis of volatile phenylpropenes in flowers. New Phytol. 2014 Nov;204(3):661-670. PMID:24985707 doi:10.1111/nph.12913
- ↑ Pan H, Zhou R, Louie GV, Muhlemann JK, Bomati EK, Bowman ME, Dudareva N, Dixon RA, Noel JP, Wang X. Structural Studies of Cinnamoyl-CoA Reductase and Cinnamyl-Alcohol Dehydrogenase, Key Enzymes of Monolignol Biosynthesis. Plant Cell. 2014 Sep 12. pii: tpc.114.127399. PMID:25217505 doi:http://dx.doi.org/10.1105/tpc.114.127399
- ↑ Pan H, Zhou R, Louie GV, Muhlemann JK, Bomati EK, Bowman ME, Dudareva N, Dixon RA, Noel JP, Wang X. Structural Studies of Cinnamoyl-CoA Reductase and Cinnamyl-Alcohol Dehydrogenase, Key Enzymes of Monolignol Biosynthesis. Plant Cell. 2014 Sep 12. pii: tpc.114.127399. PMID:25217505 doi:http://dx.doi.org/10.1105/tpc.114.127399
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