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2dre
From Proteopedia
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| - | [[Image:2dre.jpg|left|200px]] | ||
| - | + | ==Crystal structure of Water-soluble chlorophyll protein from lepidium virginicum at 2.00 angstrom resolution== | |
| - | + | <StructureSection load='2dre' size='340' side='right'caption='[[2dre]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <table><tr><td colspan='2'>[[2dre]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lepidium_virginicum Lepidium virginicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DRE 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></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=2dre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dre OCA], [https://pdbe.org/2dre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dre RCSB], [https://www.ebi.ac.uk/pdbsum/2dre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dre ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == 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/dr/2dre_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=2dre ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
A water-soluble chlorophyll-binding protein (WSCP) is the single known instance of a putative chlorophyll (Chl) carrier in green plants. Recently the photoprotective function of WSCP has been demonstrated by EPR measurements; the light-induced singlet-oxygen formation of Chl in the WSCP tetramer is about four times lower than that of unbound Chl. This paper describes the crystal structure of the WSCP-Chl complex purified from leaves of Lepidium virginicum (Virginia pepperweed) to clarify the mechanism of its photoprotective function. The WSCP-Chl complex is a homotetramer comprising four protein chains of 180 amino acids and four Chl molecules. At the center of the complex one hydrophobic cavity is formed in which all of the four Chl molecules are tightly packed and isolated from bulk solvent. With reference to the novel Chl-binding mode, we propose that the photoprotection mechanism may be based on the inhibition of physical contact between the Chl molecules and molecular oxygen. | A water-soluble chlorophyll-binding protein (WSCP) is the single known instance of a putative chlorophyll (Chl) carrier in green plants. Recently the photoprotective function of WSCP has been demonstrated by EPR measurements; the light-induced singlet-oxygen formation of Chl in the WSCP tetramer is about four times lower than that of unbound Chl. This paper describes the crystal structure of the WSCP-Chl complex purified from leaves of Lepidium virginicum (Virginia pepperweed) to clarify the mechanism of its photoprotective function. The WSCP-Chl complex is a homotetramer comprising four protein chains of 180 amino acids and four Chl molecules. At the center of the complex one hydrophobic cavity is formed in which all of the four Chl molecules are tightly packed and isolated from bulk solvent. With reference to the novel Chl-binding mode, we propose that the photoprotection mechanism may be based on the inhibition of physical contact between the Chl molecules and molecular oxygen. | ||
| - | + | Structural mechanism and photoprotective function of water-soluble chlorophyll-binding protein.,Horigome D, Satoh H, Itoh N, Mitsunaga K, Oonishi I, Nakagawa A, Uchida A J Biol Chem. 2007 Mar 2;282(9):6525-31. Epub 2006 Dec 14. PMID:17170107<ref>PMID:17170107</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2dre" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Lepidium virginicum]] | [[Category: Lepidium virginicum]] | ||
| - | + | [[Category: Horigome, D]] | |
| - | [[Category: Horigome, D | + | [[Category: Itoh, N]] |
| - | [[Category: Itoh, N | + | [[Category: Mitsunaga, K]] |
| - | [[Category: Mitsunaga, K | + | [[Category: Nakagawa, A]] |
| - | [[Category: Nakagawa, A | + | [[Category: Oonishi, I]] |
| - | [[Category: Oonishi, I | + | [[Category: Satoh, H]] |
| - | [[Category: Satoh, H | + | [[Category: Uchida, A]] |
| - | [[Category: Uchida, A | + | [[Category: Beta-trefoil]] |
| - | [[Category: | + | [[Category: Chlorophyll]] |
| - | + | [[Category: Chlorophyll carrier]] | |
| - | [[Category: | + | [[Category: Photooxidation]] |
| - | [[Category: | + | [[Category: Plant]] |
| - | [[Category: | + | [[Category: Plant protein]] |
| - | [[Category: | + | [[Category: Singlet oxygen]] |
| - | [[Category: | + | [[Category: Tetramer]] |
| - | + | [[Category: Water-soluble chlorophyll protein]] | |
| - | [[Category: | + | |
| - | [[Category: | + | |
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Current revision
Crystal structure of Water-soluble chlorophyll protein from lepidium virginicum at 2.00 angstrom resolution
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