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[[ | ==Crystal structure of circular permutated Red Fluorescent Protein mKate(cp 154-153)== | ||
<StructureSection load='3rwt' size='340' side='right' caption='[[3rwt]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3rwt]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Entacmaea_quadricolor Entacmaea quadricolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RWT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RWT FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rwa|3rwa]]</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=3rwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rwt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rwt RCSB], [http://www.ebi.ac.uk/pdbsum/3rwt PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Circular permutation of fluorescent proteins provides a substrate for the design of molecular sensors. Here we describe a systematic exploration of permutation sites for mCherry and mKate using a tandem fusion template approach. Circular permutants retaining more than 60% (mCherry) and 90% (mKate) brightness of the parent molecules are reported, as well as a quantitative evaluation of the fluorescence from neighboring mutations. Truncations of circular permutants indicated essential N- and C-terminal segments and substantial flexibility in the use of these molecules. Structural evaluation of two cp-mKate variants indicated no major conformational changes from the previously reported wild-type structure, and cis conformation of the chromophores. Four cp-mKates were identified with over 80% of native fluorescence, providing important new building blocks for sensor and complementation experiments. | |||
Circular permutation of red fluorescent proteins.,Shui B, Wang Q, Lee F, Byrnes LJ, Chudakov DM, Lukyanov SA, Sondermann H, Kotlikoff MI PLoS One. 2011;6(5):e20505. Epub 2011 May 27. PMID:21647365<ref>PMID:21647365</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Green Fluorescent Protein|Green Fluorescent Protein]] | *[[Green Fluorescent Protein|Green Fluorescent Protein]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
== | </StructureSection> | ||
< | |||
[[Category: Entacmaea quadricolor]] | [[Category: Entacmaea quadricolor]] | ||
[[Category: Sondermann, H | [[Category: Sondermann, H]] | ||
[[Category: Wang, Q | [[Category: Wang, Q]] | ||
[[Category: Circular permutated]] | [[Category: Circular permutated]] | ||
[[Category: Fluorescent protein]] | [[Category: Fluorescent protein]] | ||
Revision as of 21:35, 21 December 2014
Crystal structure of circular permutated Red Fluorescent Protein mKate(cp 154-153)Crystal structure of circular permutated Red Fluorescent Protein mKate(cp 154-153)
Structural highlights
Publication Abstract from PubMedCircular permutation of fluorescent proteins provides a substrate for the design of molecular sensors. Here we describe a systematic exploration of permutation sites for mCherry and mKate using a tandem fusion template approach. Circular permutants retaining more than 60% (mCherry) and 90% (mKate) brightness of the parent molecules are reported, as well as a quantitative evaluation of the fluorescence from neighboring mutations. Truncations of circular permutants indicated essential N- and C-terminal segments and substantial flexibility in the use of these molecules. Structural evaluation of two cp-mKate variants indicated no major conformational changes from the previously reported wild-type structure, and cis conformation of the chromophores. Four cp-mKates were identified with over 80% of native fluorescence, providing important new building blocks for sensor and complementation experiments. Circular permutation of red fluorescent proteins.,Shui B, Wang Q, Lee F, Byrnes LJ, Chudakov DM, Lukyanov SA, Sondermann H, Kotlikoff MI PLoS One. 2011;6(5):e20505. Epub 2011 May 27. PMID:21647365[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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