3svn: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3svn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SVN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SVN FirstGlance]. <br> | <table><tr><td colspan='2'>[[3svn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SVN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SVN FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NRQ:{(4Z)-4-(4-HYDROXYBENZYLIDENE)-2-[3-(METHYLTHIO)PROPANIMIDOYL]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>NRQ</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NRQ:{(4Z)-4-(4-HYDROXYBENZYLIDENE)-2-[3-(METHYLTHIO)PROPANIMIDOYL]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>NRQ</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3svo|3svo]], [[3svr|3svr]], [[3svs|3svs]], [[3svu|3svu]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3svo|3svo]], [[3svr|3svr]], [[3svs|3svs]], [[3svu|3svu]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3svn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3svn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3svn RCSB], [http://www.ebi.ac.uk/pdbsum/3svn PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3svn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3svn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3svn RCSB], [http://www.ebi.ac.uk/pdbsum/3svn PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Molecular Mechanism of a Green-Shifted, pH-Dependent Red Fluorescent Protein mKate Variant.,Wang Q, Byrnes LJ, Shui B, Rohrig UF, Singh A, Chudakov DM, Lukyanov S, Zipfel WR, Kotlikoff MI, Sondermann H PLoS One. 2011;6(8):e23513. Epub 2011 Aug 22. PMID:21887263<ref>PMID:21887263</ref> | Molecular Mechanism of a Green-Shifted, pH-Dependent Red Fluorescent Protein mKate Variant.,Wang Q, Byrnes LJ, Shui B, Rohrig UF, Singh A, Chudakov DM, Lukyanov S, Zipfel WR, Kotlikoff MI, Sondermann H PLoS One. 2011;6(8):e23513. Epub 2011 Aug 22. PMID:21887263<ref>PMID:21887263</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Synthetic construct]] | [[Category: Synthetic construct]] | ||
[[Category: Byrnes, L | [[Category: Byrnes, L]] | ||
[[Category: Sondermann, H | [[Category: Sondermann, H]] | ||
[[Category: Wang, Q | [[Category: Wang, Q]] | ||
[[Category: Fluorescent protein]] | [[Category: Fluorescent protein]] | ||
[[Category: Fluoresent protein]] | [[Category: Fluoresent protein]] | ||
[[Category: Ph sensor]] | [[Category: Ph sensor]] | ||
Revision as of 12:30, 4 January 2015
Crystal structure of mKate S158A mutant at pH 7.5Crystal structure of mKate S158A mutant at pH 7.5
Structural highlights
Publication Abstract from PubMedFluorescent proteins that can switch between distinct colors have contributed significantly to modern biomedical imaging technologies and molecular cell biology. Here we report the identification and biochemical analysis of a green-shifted red fluorescent protein variant GmKate, produced by the introduction of two mutations into mKate. Although the mutations decrease the overall brightness of the protein, GmKate is subject to pH-dependent, reversible green-to-red color conversion. At physiological pH, GmKate absorbs blue light (445 nm) and emits green fluorescence (525 nm). At pH above 9.0, GmKate absorbs 598 nm light and emits 646 nm, far-red fluorescence, similar to its sequence homolog mNeptune. Based on optical spectra and crystal structures of GmKate in its green and red states, the reversible color transition is attributed to the different protonation states of the cis-chromophore, an interpretation that was confirmed by quantum chemical calculations. Crystal structures reveal potential hydrogen bond networks around the chromophore that may facilitate the protonation switch, and indicate a molecular basis for the unusual bathochromic shift observed at high pH. This study provides mechanistic insights into the color tuning of mKate variants, which may aid the development of green-to-red color-convertible fluorescent sensors, and suggests GmKate as a prototype of genetically encoded pH sensors for biological studies. Molecular Mechanism of a Green-Shifted, pH-Dependent Red Fluorescent Protein mKate Variant.,Wang Q, Byrnes LJ, Shui B, Rohrig UF, Singh A, Chudakov DM, Lukyanov S, Zipfel WR, Kotlikoff MI, Sondermann H PLoS One. 2011;6(8):e23513. Epub 2011 Aug 22. PMID:21887263[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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