7rrk: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='7rrk' size='340' side='right'caption='[[7rrk]], [[Resolution|resolution]] 1.93Å' scene=''> | <StructureSection load='7rrk' size='340' side='right'caption='[[7rrk]], [[Resolution|resolution]] 1.93Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7rrk]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RRK FirstGlance]. <br> | <table><tr><td colspan='2'>[[7rrk]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Echinophyllia_sp._SC22 Echinophyllia sp. SC22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RRK FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.929Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GYC:[(4Z)-2-[(1R)-1-AMINO-2-MERCAPTOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYC</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=7rrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rrk OCA], [https://pdbe.org/7rrk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rrk RCSB], [https://www.ebi.ac.uk/pdbsum/7rrk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rrk ProSAT]</span></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=7rrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rrk OCA], [https://pdbe.org/7rrk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rrk RCSB], [https://www.ebi.ac.uk/pdbsum/7rrk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rrk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5TLG6_9CNID Q5TLG6_9CNID] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 16: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 7rrk" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7rrk" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Dronpa|Dronpa]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Echinophyllia sp. SC22]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Boxer | [[Category: Boxer SG]] | ||
[[Category: Lin | [[Category: Lin C-Y]] | ||
[[Category: Mathews | [[Category: Mathews II]] | ||
[[Category: Romei | [[Category: Romei MG]] | ||
Latest revision as of 19:36, 18 October 2023
Crystal structure of fast switching M159E mutant of fluorescent protein Dronpa (Dronpa2)Crystal structure of fast switching M159E mutant of fluorescent protein Dronpa (Dronpa2)
Structural highlights
FunctionPublication Abstract from PubMedThe past decades have witnessed an explosion of de novo protein designs with a remarkable range of scaffolds. It remains challenging, however, to design catalytic functions that are competitive with naturally occurring counterparts as well as biomimetic or nonbiological catalysts. Although directed evolution often offers efficient solutions, the fitness landscape remains opaque. Green fluorescent protein (GFP), which has revolutionized biological imaging and assays, is one of the most redesigned proteins. While not an enzyme in the conventional sense, GFPs feature competing excited-state decay pathways with the same steric and electrostatic origins as conventional ground-state catalysts, and they exert exquisite control over multiple reaction outcomes through the same principles. Thus, GFP is an "excited-state enzyme". Herein we show that rationally designed mutants and hybrids that contain environmental mutations and substituted chromophores provide the basis for a quantitative model and prediction that describes the influence of sterics and electrostatics on excited-state catalysis of GFPs. As both perturbations can selectively bias photoisomerization pathways, GFPs with fluorescence quantum yields (FQYs) and photoswitching characteristics tailored for specific applications could be predicted and then demonstrated. The underlying energetic landscape, readily accessible via spectroscopy for GFPs, offers an important missing link in the design of protein function that is generalizable to catalyst design. Energetic Basis and Design of Enzyme Function Demonstrated Using GFP, an Excited-State Enzyme.,Lin CY, Romei MG, Mathews II, Boxer SG J Am Chem Soc. 2022 Mar 9;144(9):3968-3978. doi: 10.1021/jacs.1c12305. Epub 2022 , Feb 24. PMID:35200017[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||