1ppr
From Proteopedia
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== Structural highlights == | == 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> | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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> | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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]. | </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="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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1ppr" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Amphidinium carterae]] | [[Category: Amphidinium carterae]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Diederichs | + | [[Category: Diederichs K]] |
| - | [[Category: Hofmann | + | [[Category: Hofmann E]] |
| - | [[Category: Welte | + | [[Category: Welte W]] |
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Current revision
PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE
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