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[[Image:1gp5.jpg|left|200px]]<br /><applet load="1gp5" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1gp5, resolution 2.2&Aring;" />
'''ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA COMPLEXED WITH TRANS-DIHYDROQUERCETIN'''<br />


==Overview==
==Anthocyanidin synthase from Arabidopsis thaliana complexed with trans-dihydroquercetin==
Flavonoids are common colorants in plants and have long-established, biomedicinal properties. Anthocyanidin synthase (ANS), a 2-oxoglutarate, iron-dependent oxygenase, catalyzes the penultimate step in the, biosynthesis of the anthocyanin class of flavonoids. The crystal structure, of ANS reveals a multicomponent active site containing metal, cosubstrate, and two molecules of a substrate analog (dihydroquercetin). An additional, structure obtained after 30 min exposure to dioxygen is consistent with, the oxidation of the dihydroquercetin to quercetin and the concomitant, decarboxylation of 2-oxoglutarate to succinate. Together with in vitro, studies, the crystal structures suggest a mechanism for ANS-catalyzed, anthocyanidin formation from the natural leucoanthocyanidin substrates, involving stereoselective C-3 hydroxylation. The structure of ANS provides, a template for the ubiquitous family of plant nonhaem oxygenases for, future engineering and inhibition studies.
<StructureSection load='1gp5' size='340' side='right'caption='[[1gp5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gp5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GP5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=DH2:(2S,3S)-2-(3,4-DIHYDROXYPHENYL)-3,5,7-TRIHYDROXY-2,3-DIHYDRO-4H-CHROMEN-4-ONE'>DH2</scene>, <scene name='pdbligand=DQH:(2R,3R)-2-(3,4-DIHYDROXYPHENYL)-3,5,7-TRIHYDROXY-2,3-DIHYDRO-4H-CHROMEN-4-ONE'>DQH</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></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=1gp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gp5 OCA], [https://pdbe.org/1gp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gp5 RCSB], [https://www.ebi.ac.uk/pdbsum/1gp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gp5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LDOX_ARATH LDOX_ARATH] Involved in anthocyanin and protoanthocyanidin biosynthesis by catalyzing the oxidation of leucoanthocyanidins into anthocyanidins. Possesses low flavonol synthase activity in vitro towards dihydrokaempferol and dihydroquercetin producing kaempferol and quercitin, respectively.<ref>PMID:12940955</ref> <ref>PMID:16153644</ref> <ref>PMID:19433090</ref> <ref>PMID:21683773</ref> <ref>PMID:16106293</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/1gp5_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gp5 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Flavonoids are common colorants in plants and have long-established biomedicinal properties. Anthocyanidin synthase (ANS), a 2-oxoglutarate iron-dependent oxygenase, catalyzes the penultimate step in the biosynthesis of the anthocyanin class of flavonoids. The crystal structure of ANS reveals a multicomponent active site containing metal, cosubstrate, and two molecules of a substrate analog (dihydroquercetin). An additional structure obtained after 30 min exposure to dioxygen is consistent with the oxidation of the dihydroquercetin to quercetin and the concomitant decarboxylation of 2-oxoglutarate to succinate. Together with in vitro studies, the crystal structures suggest a mechanism for ANS-catalyzed anthocyanidin formation from the natural leucoanthocyanidin substrates involving stereoselective C-3 hydroxylation. The structure of ANS provides a template for the ubiquitous family of plant nonhaem oxygenases for future engineering and inhibition studies.


==About this Structure==
Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana.,Wilmouth RC, Turnbull JJ, Welford RW, Clifton IJ, Prescott AG, Schofield CJ Structure. 2002 Jan;10(1):93-103. PMID:11796114<ref>PMID:11796114</ref>
1GP5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with FE, AKG, MES, DQH and DH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=IRN:2og Binding Site For Chain A'>IRN</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GP5 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana., Wilmouth RC, Turnbull JJ, Welford RW, Clifton IJ, Prescott AG, Schofield CJ, Structure. 2002 Jan;10(1):93-103. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11796114 11796114]
</div>
<div class="pdbe-citations 1gp5" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Clifton, I.J.]]
[[Category: Clifton IJ]]
[[Category: Prescott, A.G.]]
[[Category: Prescott AG]]
[[Category: Schofield, C.J.]]
[[Category: Schofield CJ]]
[[Category: Turnbull, J.J.]]
[[Category: Turnbull JJ]]
[[Category: Welford, R.W.D.]]
[[Category: Welford RWD]]
[[Category: Wilmouth, R.C.]]
[[Category: Wilmouth RC]]
[[Category: AKG]]
[[Category: DH2]]
[[Category: DQH]]
[[Category: FE]]
[[Category: MES]]
[[Category: 2-oxoglutarate dependent dioxygenase]]
[[Category: flavonoid biosynthesis]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:28:56 2007''

Latest revision as of 15:02, 13 December 2023

Anthocyanidin synthase from Arabidopsis thaliana complexed with trans-dihydroquercetinAnthocyanidin synthase from Arabidopsis thaliana complexed with trans-dihydroquercetin

Structural highlights

1gp5 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LDOX_ARATH Involved in anthocyanin and protoanthocyanidin biosynthesis by catalyzing the oxidation of leucoanthocyanidins into anthocyanidins. Possesses low flavonol synthase activity in vitro towards dihydrokaempferol and dihydroquercetin producing kaempferol and quercitin, respectively.[1] [2] [3] [4] [5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Flavonoids are common colorants in plants and have long-established biomedicinal properties. Anthocyanidin synthase (ANS), a 2-oxoglutarate iron-dependent oxygenase, catalyzes the penultimate step in the biosynthesis of the anthocyanin class of flavonoids. The crystal structure of ANS reveals a multicomponent active site containing metal, cosubstrate, and two molecules of a substrate analog (dihydroquercetin). An additional structure obtained after 30 min exposure to dioxygen is consistent with the oxidation of the dihydroquercetin to quercetin and the concomitant decarboxylation of 2-oxoglutarate to succinate. Together with in vitro studies, the crystal structures suggest a mechanism for ANS-catalyzed anthocyanidin formation from the natural leucoanthocyanidin substrates involving stereoselective C-3 hydroxylation. The structure of ANS provides a template for the ubiquitous family of plant nonhaem oxygenases for future engineering and inhibition studies.

Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana.,Wilmouth RC, Turnbull JJ, Welford RW, Clifton IJ, Prescott AG, Schofield CJ Structure. 2002 Jan;10(1):93-103. PMID:11796114[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Abrahams S, Lee E, Walker AR, Tanner GJ, Larkin PJ, Ashton AR. The Arabidopsis TDS4 gene encodes leucoanthocyanidin dioxygenase (LDOX) and is essential for proanthocyanidin synthesis and vacuole development. Plant J. 2003 Sep;35(5):624-36. PMID:12940955
  2. ↑ Welford RW, Kirkpatrick JM, McNeill LA, Puri M, Oldham NJ, Schofield CJ. Incorporation of oxygen into the succinate co-product of iron(II) and 2-oxoglutarate dependent oxygenases from bacteria, plants and humans. FEBS Lett. 2005 Sep 26;579(23):5170-4. PMID:16153644 doi:10.1016/j.febslet.2005.08.033
  3. ↑ Preuss A, Stracke R, Weisshaar B, Hillebrecht A, Matern U, Martens S. Arabidopsis thaliana expresses a second functional flavonol synthase. FEBS Lett. 2009 Jun 18;583(12):1981-6. doi: 10.1016/j.febslet.2009.05.006. Epub, 2009 May 10. PMID:19433090 doi:10.1016/j.febslet.2009.05.006
  4. ↑ Appelhagen I, Jahns O, Bartelniewoehner L, Sagasser M, Weisshaar B, Stracke R. Leucoanthocyanidin Dioxygenase in Arabidopsis thaliana: characterization of mutant alleles and regulation by MYB-BHLH-TTG1 transcription factor complexes. Gene. 2011 Sep 15;484(1-2):61-8. doi: 10.1016/j.gene.2011.05.031. Epub 2011 Jun, 12. PMID:21683773 doi:10.1016/j.gene.2011.05.031
  5. ↑ Welford RW, Clifton IJ, Turnbull JJ, Wilson SC, Schofield CJ. Structural and mechanistic studies on anthocyanidin synthase catalysed oxidation of flavanone substrates: the effect of C-2 stereochemistry on product selectivity and mechanism. Org Biomol Chem. 2005 Sep 7;3(17):3117-26. Epub 2005 Aug 1. PMID:16106293 doi:http://dx.doi.org/10.1039/b507153d
  6. ↑ Wilmouth RC, Turnbull JJ, Welford RW, Clifton IJ, Prescott AG, Schofield CJ. Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana. Structure. 2002 Jan;10(1):93-103. PMID:11796114

1gp5, resolution 2.20Å

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