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2ddc
From Proteopedia
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| - | [[Image:2ddc.png|left|200px]] | ||
| - | + | ==Unique behavior of a histidine responsible for an engineered green-to-red photoconversion process== | |
| + | <StructureSection load='2ddc' size='340' side='right'caption='[[2ddc]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2ddc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dipsastraea_favus Dipsastraea favus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DDC 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]] 1.55Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CR8:2-[1-AMINO-2-(1H-IMIDAZOL-5-YL)ETHYL]-1-(CARBOXYMETHYL)-4-[(4-OXOCYCLOHEXA-2,5-DIEN-1-YLIDENE)METHYL]-1H-IMIDAZOL-5-OLATE'>CR8</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=2ddc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ddc OCA], [https://pdbe.org/2ddc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ddc RCSB], [https://www.ebi.ac.uk/pdbsum/2ddc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ddc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q53UG8_DIPFA Q53UG8_DIPFA] | ||
| + | == 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/dd/2ddc_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=2ddc ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | KikGR is a fluorescent protein engineered to display green-to-red photoconvertibility that is induced by irradiation with ultraviolet or violet light. Similar to Kaede and EosFP, two naturally occurring photoconvertible proteins, KikGR contains a His(62)-Tyr(63)-Gly(64) tripeptide sequence, which forms a green chromophore that can be photoconverted to a red one via formal beta-elimination and subsequent extension of a pi-conjugated system. Using a crystallizable variant of KikGR, we determined the structures of both the green and red state at 1.55 A resolution. The double bond between His(62)-C(alpha) and His(62)-C(beta) in the red chromophore is in a cis configuration, indicating that rotation along the His(62) C(alpha)-C(beta) bond occurs following cleavage of the His(62) N(alpha)-C(alpha) bond. This structural rearrangement provides evidence that the beta-elimination reaction governing the green-to-red photoconversion of KikGR follows an E1 (elimination, unimolecular) mechanism. | ||
| - | + | The E1 mechanism in photo-induced beta-elimination reactions for green-to-red conversion of fluorescent proteins.,Tsutsui H, Shimizu H, Mizuno H, Nukina N, Furuta T, Miyawaki A Chem Biol. 2009 Nov 25;16(11):1140-7. PMID:19942137<ref>PMID:19942137</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2ddc" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | + | *[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |
| - | + | == References == | |
| - | *[[Green Fluorescent Protein|Green Fluorescent Protein]] | + | <references/> |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Dipsastraea favus]] | |
| - | == | + | [[Category: Large Structures]] |
| - | < | + | [[Category: Miyawaki A]] |
| - | [[Category: | + | [[Category: Nukina N]] |
| - | [[Category: Miyawaki | + | [[Category: Shimizu H]] |
| - | [[Category: Nukina | + | [[Category: Tsutsui H]] |
| - | [[Category: Shimizu | + | |
| - | [[Category: Tsutsui | + | |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Unique behavior of a histidine responsible for an engineered green-to-red photoconversion process
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