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| | <StructureSection load='3npe' size='340' side='right'caption='[[3npe]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='3npe' size='340' side='right'caption='[[3npe]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3npe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Maize Maize]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NPE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3npe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NPE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP14 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4577 MAIZE])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/9-cis-epoxycarotenoid_dioxygenase 9-cis-epoxycarotenoid dioxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.51 1.13.11.51] </span></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=3npe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3npe OCA], [https://pdbe.org/3npe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3npe RCSB], [https://www.ebi.ac.uk/pdbsum/3npe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3npe ProSAT]</span></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=3npe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3npe OCA], [https://pdbe.org/3npe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3npe RCSB], [https://www.ebi.ac.uk/pdbsum/3npe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3npe ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/NCED1_MAIZE NCED1_MAIZE]] Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids. Not active on the all-trans isomers of violaxanthin and neoxanthin. Contributes probably to abscisic acid synthesis for the induction of seed dormancy.<ref>PMID:9342392</ref> <ref>PMID:9188535</ref> <ref>PMID:20884803</ref>
| + | [https://www.uniprot.org/uniprot/NCED1_MAIZE NCED1_MAIZE] Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids. Not active on the all-trans isomers of violaxanthin and neoxanthin. Contributes probably to abscisic acid synthesis for the induction of seed dormancy.<ref>PMID:9342392</ref> <ref>PMID:9188535</ref> <ref>PMID:20884803</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 9-cis-epoxycarotenoid dioxygenase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Maize]] | + | [[Category: Zea mays]] |
| - | [[Category: Amzel, L M]] | + | [[Category: Amzel LM]] |
| - | [[Category: Gabelli, S B]] | + | [[Category: Gabelli SB]] |
| - | [[Category: Messing, S A]] | + | [[Category: Messing SA]] |
| - | [[Category: Abscisic acid]]
| + | |
| - | [[Category: Dioxygenase]]
| + | |
| - | [[Category: Non heme iron]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Seven blade beta propeller]]
| + | |
| Structural highlights
Function
NCED1_MAIZE Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids. Not active on the all-trans isomers of violaxanthin and neoxanthin. Contributes probably to abscisic acid synthesis for the induction of seed dormancy.[1] [2] [3]
Publication Abstract from PubMed
The key regulatory step in the biosynthesis of abscisic acid (ABA), a hormone central to the regulation of several important processes in plants, is the oxidative cleavage of the 11,12 double bond of a 9-cis-epoxycarotenoid. The enzyme viviparous14 (VP14) performs this cleavage in maize (Zea mays), making it a target for the rational design of novel chemical agents and genetic modifications that improve plant behavior through the modulation of ABA levels. The structure of VP14, determined to 3.2-A resolution, provides both insight into the determinants of regio- and stereospecificity of this enzyme and suggests a possible mechanism for oxidative cleavage. Furthermore, mutagenesis of the distantly related CCD1 of maize shows how the VP14 structure represents a template for all plant carotenoid cleavage dioxygenases (CCDs). In addition, the structure suggests how VP14 associates with the membrane as a way of gaining access to its membrane soluble substrate.
Structural insights into maize viviparous14, a key enzyme in the biosynthesis of the phytohormone abscisic acid.,Messing SA, Gabelli SB, Echeverria I, Vogel JT, Guan JC, Tan BC, Klee HJ, McCarty DR, Amzel LM Plant Cell. 2010 Sep;22(9):2970-80. Epub 2010 Sep 30. PMID:20884803[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tan BC, Schwartz SH, Zeevaart JA, McCarty DR. Genetic control of abscisic acid biosynthesis in maize. Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):12235-40. PMID:9342392
- ↑ Schwartz SH, Tan BC, Gage DA, Zeevaart JA, McCarty DR. Specific oxidative cleavage of carotenoids by VP14 of maize. Science. 1997 Jun 20;276(5320):1872-4. PMID:9188535
- ↑ Messing SA, Gabelli SB, Echeverria I, Vogel JT, Guan JC, Tan BC, Klee HJ, McCarty DR, Amzel LM. Structural insights into maize viviparous14, a key enzyme in the biosynthesis of the phytohormone abscisic acid. Plant Cell. 2010 Sep;22(9):2970-80. Epub 2010 Sep 30. PMID:20884803 doi:10.1105/tpc.110.074815
- ↑ Messing SA, Gabelli SB, Echeverria I, Vogel JT, Guan JC, Tan BC, Klee HJ, McCarty DR, Amzel LM. Structural insights into maize viviparous14, a key enzyme in the biosynthesis of the phytohormone abscisic acid. Plant Cell. 2010 Sep;22(9):2970-80. Epub 2010 Sep 30. PMID:20884803 doi:10.1105/tpc.110.074815
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