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New page: left|200px<br /><applet load="1ppr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ppr, resolution 2.0Å" /> '''PERIDININ-CHLOROPHYLL...
 
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[[Image:1ppr.gif|left|200px]]<br /><applet load="1ppr" size="450" color="white" frame="true" align="right" spinBox="true"
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'''PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE'''<br />


==Overview==
==PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE==
Peridinin-chlorophyll-protein, a water-soluble light-harvesting complex, that has a blue-green absorbing carotenoid as its main pigment, is present, in most photosynthetic dinoflagellates. Its high-resolution (2.0 angstrom), x-ray structure reveals a noncrystallographic trimer in which each, polypeptide contains an unusual jellyroll fold of the alpha-helical amino-, and carboxyl-terminal domains. These domains constitute a scaffold with, pseudo-twofold symmetry surrounding a hydrophobic cavity filled by two, lipid, eight peridinin, and two chlorophyll a molecules. The structural, basis for efficient excitonic energy transfer from peridinin to, chlorophyll is found in the clustering of peridinins around the, chlorophylls at van der Waals distances.
<StructureSection load='1ppr' size='340' side='right'caption='[[1ppr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ppr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Amphidinium_carterae Amphidinium carterae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PPR 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=DGD:DIGALACTOSYL+DIACYL+GLYCEROL+(DGDG)'>DGD</scene>, <scene name='pdbligand=PID:PERIDININ'>PID</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=1ppr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ppr OCA], [https://pdbe.org/1ppr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ppr RCSB], [https://www.ebi.ac.uk/pdbsum/1ppr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ppr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PCP1_AMPCA PCP1_AMPCA] Water-soluble antenna for capture of solar energy in the blue-green range. Peridinin is an asymmetric carotenoid.
== 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/pp/1ppr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ppr ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peridinin-chlorophyll-protein, a water-soluble light-harvesting complex that has a blue-green absorbing carotenoid as its main pigment, is present in most photosynthetic dinoflagellates. Its high-resolution (2.0 angstrom) x-ray structure reveals a noncrystallographic trimer in which each polypeptide contains an unusual jellyroll fold of the alpha-helical amino- and carboxyl-terminal domains. These domains constitute a scaffold with pseudo-twofold symmetry surrounding a hydrophobic cavity filled by two lipid, eight peridinin, and two chlorophyll a molecules. The structural basis for efficient excitonic energy transfer from peridinin to chlorophyll is found in the clustering of peridinins around the chlorophylls at van der Waals distances.


==About this Structure==
Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae.,Hofmann E, Wrench PM, Sharples FP, Hiller RG, Welte W, Diederichs K Science. 1996 Jun 21;272(5269):1788-91. PMID:8650577<ref>PMID:8650577</ref>
1PPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Amphidinium_carterae Amphidinium carterae] with CLA, PID and DGD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PPR OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae., Hofmann E, Wrench PM, Sharples FP, Hiller RG, Welte W, Diederichs K, Science. 1996 Jun 21;272(5269):1788-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8650577 8650577]
</div>
<div class="pdbe-citations 1ppr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Amphidinium carterae]]
[[Category: Amphidinium carterae]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Diederichs, K.]]
[[Category: Diederichs K]]
[[Category: Hofmann, E.]]
[[Category: Hofmann E]]
[[Category: Welte, W.]]
[[Category: Welte W]]
[[Category: CLA]]
[[Category: DGD]]
[[Category: PID]]
[[Category: carotenoids]]
[[Category: dinoflagellates]]
[[Category: light harvesting protein]]
[[Category: photosynthesis]]
 
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Latest revision as of 06:56, 13 August 2026

PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE

1ppr, resolution 2.00Å

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