5wj2: Difference between revisions
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<StructureSection load='5wj2' size='340' side='right' caption='[[5wj2]], [[Resolution|resolution]] 2.41Å' scene=''> | <StructureSection load='5wj2' size='340' side='right' caption='[[5wj2]], [[Resolution|resolution]] 2.41Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5wj2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WJ2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5wj2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeqvi Aeqvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WJ2 FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CR2:{(4Z)-2-(AMINOMETHYL)-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CR2</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=CR2:{(4Z)-2-(AMINOMETHYL)-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CR2</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cfp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 AEQVI])</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=5wj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wj2 OCA], [http://pdbe.org/5wj2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wj2 RCSB], [http://www.ebi.ac.uk/pdbsum/5wj2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wj2 ProSAT]</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=5wj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wj2 OCA], [http://pdbe.org/5wj2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wj2 RCSB], [http://www.ebi.ac.uk/pdbsum/5wj2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wj2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We have determined the crystal structure of Clover, one of the brightest fluorescent proteins, and found that its T203H/S65G mutations relative to wild-type GFP lock the critical E222 side chain in a fixed configuration that mimics the major conformer of that in EGFP. The resulting equilibrium shift to the predominantly deprotonated chromophore increases the extinction coefficient (EC), opposes photoactivation, and is responsible for the bathochromic shift. Clover's brightness can further be attributed to a pi-pi stacking interaction between H203 and the chromophore. Consistent with these observations, the Clover G65S mutant reversed the equilibrium shift, dramatically decreased the EC, and made Clover photoactivatable under conditions that activated photoactivatable GFP. Using the Clover structure, we rationally engineered a non-photoactivatable redox sensor, roClover1, and determined its structure as well as that of its parental template, roClover0.1. These high-resolution structures provide deeper insights into structure-function relationships in GFPs and may aid the development of excitation-improved ratiometric biosensors. | |||
Crystal Structure of Green Fluorescent Protein Clover and Design of Clover-Based Redox Sensors.,Campbell BC, Petsko GA, Liu CF Structure. 2017 Dec 27. pii: S0969-2126(17)30405-7. doi:, 10.1016/j.str.2017.12.006. PMID:29307487<ref>PMID:29307487</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5wj2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aeqvi]] | |||
[[Category: Campbell, B C]] | [[Category: Campbell, B C]] | ||
[[Category: Liu, C]] | [[Category: Liu, C]] | ||
Revision as of 23:50, 24 January 2018
Crystal structure of the green fluorescent protein CloverCrystal structure of the green fluorescent protein Clover
Structural highlights
Publication Abstract from PubMedWe have determined the crystal structure of Clover, one of the brightest fluorescent proteins, and found that its T203H/S65G mutations relative to wild-type GFP lock the critical E222 side chain in a fixed configuration that mimics the major conformer of that in EGFP. The resulting equilibrium shift to the predominantly deprotonated chromophore increases the extinction coefficient (EC), opposes photoactivation, and is responsible for the bathochromic shift. Clover's brightness can further be attributed to a pi-pi stacking interaction between H203 and the chromophore. Consistent with these observations, the Clover G65S mutant reversed the equilibrium shift, dramatically decreased the EC, and made Clover photoactivatable under conditions that activated photoactivatable GFP. Using the Clover structure, we rationally engineered a non-photoactivatable redox sensor, roClover1, and determined its structure as well as that of its parental template, roClover0.1. These high-resolution structures provide deeper insights into structure-function relationships in GFPs and may aid the development of excitation-improved ratiometric biosensors. Crystal Structure of Green Fluorescent Protein Clover and Design of Clover-Based Redox Sensors.,Campbell BC, Petsko GA, Liu CF Structure. 2017 Dec 27. pii: S0969-2126(17)30405-7. doi:, 10.1016/j.str.2017.12.006. PMID:29307487[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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