7ugt: Difference between revisions
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==Crystal structure of hyperfolder fluorescent protein FOLD6== | |||
<StructureSection load='7ugt' size='340' side='right'caption='[[7ugt]], [[Resolution|resolution]] 1.21Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7ugt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UGT 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]] 1.21Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ugt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ugt OCA], [https://pdbe.org/7ugt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ugt RCSB], [https://www.ebi.ac.uk/pdbsum/7ugt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ugt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A059PIR9_AEQVI A0A059PIR9_AEQVI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We report the rational engineering of a remarkably stable yellow fluorescent protein (YFP), 'hyperfolder YFP' (hfYFP), that withstands chaotropic conditions that denature most biological structures within seconds, including superfolder green fluorescent protein (GFP). hfYFP contains no cysteines, is chloride insensitive and tolerates aldehyde and osmium tetroxide fixation better than common fluorescent proteins, enabling its use in expansion and electron microscopies. We solved crystal structures of hfYFP (to 1.7-A resolution), a monomeric variant, monomeric hyperfolder YFP (1.6 A) and an mGreenLantern mutant (1.2 A), and then rationally engineered highly stable 405-nm-excitable GFPs, large Stokes shift (LSS) monomeric GFP (LSSmGFP) and LSSA12 from these structures. Lastly, we directly exploited the chemical stability of hfYFP and LSSmGFP by devising a fluorescence-assisted protein purification strategy enabling all steps of denaturing affinity chromatography to be visualized using ultraviolet or blue light. hfYFP and LSSmGFP represent a new generation of robustly stable fluorescent proteins developed for advanced biotechnological applications. | |||
Chemically stable fluorescent proteins for advanced microscopy.,Campbell BC, Paez-Segala MG, Looger LL, Petsko GA, Liu CF Nat Methods. 2022 Dec;19(12):1612-1621. doi: 10.1038/s41592-022-01660-7. Epub , 2022 Nov 7. PMID:36344833<ref>PMID:36344833</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7ugt" style="background-color:#fffaf0;"></div> | ||
[[Category: Campbell | |||
[[Category: Liu | ==See Also== | ||
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aequorea victoria]] | |||
[[Category: Large Structures]] | |||
[[Category: Campbell BC]] | |||
[[Category: Liu CF]] | |||
[[Category: Petsko GA]] | |||
Latest revision as of 17:06, 6 November 2024
Crystal structure of hyperfolder fluorescent protein FOLD6Crystal structure of hyperfolder fluorescent protein FOLD6
Structural highlights
FunctionPublication Abstract from PubMedWe report the rational engineering of a remarkably stable yellow fluorescent protein (YFP), 'hyperfolder YFP' (hfYFP), that withstands chaotropic conditions that denature most biological structures within seconds, including superfolder green fluorescent protein (GFP). hfYFP contains no cysteines, is chloride insensitive and tolerates aldehyde and osmium tetroxide fixation better than common fluorescent proteins, enabling its use in expansion and electron microscopies. We solved crystal structures of hfYFP (to 1.7-A resolution), a monomeric variant, monomeric hyperfolder YFP (1.6 A) and an mGreenLantern mutant (1.2 A), and then rationally engineered highly stable 405-nm-excitable GFPs, large Stokes shift (LSS) monomeric GFP (LSSmGFP) and LSSA12 from these structures. Lastly, we directly exploited the chemical stability of hfYFP and LSSmGFP by devising a fluorescence-assisted protein purification strategy enabling all steps of denaturing affinity chromatography to be visualized using ultraviolet or blue light. hfYFP and LSSmGFP represent a new generation of robustly stable fluorescent proteins developed for advanced biotechnological applications. Chemically stable fluorescent proteins for advanced microscopy.,Campbell BC, Paez-Segala MG, Looger LL, Petsko GA, Liu CF Nat Methods. 2022 Dec;19(12):1612-1621. doi: 10.1038/s41592-022-01660-7. Epub , 2022 Nov 7. PMID:36344833[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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