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New page: left|200px<br /><applet load="2ddd" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ddd, resolution 1.55Å" /> '''Unique behavior of a... |
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== | ==Unique behavior of a histidine responsible for an engineered green-to-red photoconversion process== | ||
<StructureSection load='2ddd' size='340' side='right'caption='[[2ddd]], [[Resolution|resolution]] 1.55Å' scene=''> | |||
== Structural highlights == | |||
[ | <table><tr><td colspan='2'>[[2ddd]] 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=2DDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DDD 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=2ddd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ddd OCA], [https://pdbe.org/2ddd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ddd RCSB], [https://www.ebi.ac.uk/pdbsum/2ddd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ddd 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/2ddd_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=2ddd 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 2ddd" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Dipsastraea favus]] | |||
[[Category: Large Structures]] | |||
[[Category: Miyawaki A]] | |||
[[Category: Nukina N]] | |||
[[Category: Shimizu H]] | |||
[[Category: Tsutsui H]] | |||
Latest revision as of 10:55, 30 October 2024
Unique behavior of a histidine responsible for an engineered green-to-red photoconversion processUnique behavior of a histidine responsible for an engineered green-to-red photoconversion process
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedKikGR 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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