View source for 1ppr


==PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE==
<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].
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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Amphidinium carterae]]
[[Category: Large Structures]]
[[Category: Diederichs K]]
[[Category: Hofmann E]]
[[Category: Welte W]]