3mg3
From Proteopedia
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| - | {{STRUCTURE_3mg3| PDB=3mg3 | SCENE= }} | ||
| - | ===Crystal structure of the orange carotenoid protein R155L mutant from cyanobacteria synechocystis sp. PCC 6803=== | ||
| - | {{ABSTRACT_PUBMED_20368334}} | ||
| - | == | + | ==Crystal structure of the orange carotenoid protein R155L mutant from cyanobacteria synechocystis sp. PCC 6803== |
| - | [[http://www.uniprot.org/uniprot/OCP_SYNY3 OCP_SYNY3 | + | <StructureSection load='3mg3' size='340' side='right'caption='[[3mg3]], [[Resolution|resolution]] 1.70Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3mg3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3i1x 3i1x]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MG3 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]] 1.702Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ECH:BETA,BETA-CAROTEN-4-ONE'>ECH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3mg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mg3 OCA], [https://pdbe.org/3mg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mg3 RCSB], [https://www.ebi.ac.uk/pdbsum/3mg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mg3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/OCP_SYNY3 OCP_SYNY3] Acts as a photo-protectant. Essential for inhibiting white and blue-green light non-photochemical quenching (NPQ). Binding carotenoids improves OCP's intrinsic photoprotectant activity by broadening its absorption spectrum and facilitating the dissipation of absorbed energy.<ref>PMID:16531492</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/mg/3mg3_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=3mg3 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The photoprotective processes of photosynthetic organisms involve the dissipation of excess absorbed light energy as heat. Photoprotection in cyanobacteria is mechanistically distinct from that in plants; it involves the orange carotenoid protein (OCP), a water-soluble protein containing a single carotenoid. The OCP is a new member of the family of blue light-photoactive proteins; blue-green light triggers the OCP-mediated photoprotective response. Here we report structural and functional characterization of the wild type and two mutant forms of the OCP, from the model organism Synechocystis PCC6803. The structural analysis provides high resolution detail of the carotenoid-protein interactions that underlie the optical properties of the OCP, unique among carotenoid-proteins in binding a single pigment per polypeptide chain. Collectively, these data implicate several key amino acids in the function of the OCP and reveal that the photoconversion and photoprotective responses of the OCP to blue-green light can be decoupled. | ||
| - | + | Structural determinants underlying photoprotection in the photoactive orange carotenoid protein of cyanobacteria.,Wilson A, Kinney JN, Zwart PH, Punginelli C, D'Haene S, Perreau F, Klein MG, Kirilovsky D, Kerfeld CA J Biol Chem. 2010 Jun 11;285(24):18364-75. Epub 2010 Apr 5. PMID:20368334<ref>PMID:20368334</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | [[Category: Synechocystis sp.]] | + | <div class="pdbe-citations 3mg3" style="background-color:#fffaf0;"></div> |
| - | [[Category: Haen | + | == References == |
| - | [[Category: Kerfeld | + | <references/> |
| - | [[Category: Kinney | + | __TOC__ |
| - | [[Category: Kirilovsky | + | </StructureSection> |
| - | [[Category: Klein | + | [[Category: Large Structures]] |
| - | [[Category: Perreau | + | [[Category: Synechocystis sp. PCC 6803]] |
| - | [[Category: Punginelli | + | [[Category: D'Haen S]] |
| - | [[Category: Wilson | + | [[Category: Kerfeld CA]] |
| - | [[Category: Zwart | + | [[Category: Kinney J]] |
| - | + | [[Category: Kirilovsky D]] | |
| - | + | [[Category: Klein MG]] | |
| - | + | [[Category: Perreau F]] | |
| + | [[Category: Punginelli C]] | ||
| + | [[Category: Wilson A]] | ||
| + | [[Category: Zwart PH]] | ||
Current revision
Crystal structure of the orange carotenoid protein R155L mutant from cyanobacteria synechocystis sp. PCC 6803
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