1oxe: Difference between revisions
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<StructureSection load='1oxe' size='340' side='right'caption='[[1oxe]], [[Resolution|resolution]] 1.15Å' scene=''> | <StructureSection load='1oxe' size='340' side='right'caption='[[1oxe]], [[Resolution|resolution]] 1.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1oxe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1oxe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cfp_marker_plasmid_pWM1009 Cfp marker plasmid pWM1009]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OXE 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]] 1.15Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRF:[(4Z)-2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(1H-INDOL-3-YLMETHYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>CRF</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=1oxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxe OCA], [https://pdbe.org/1oxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oxe RCSB], [https://www.ebi.ac.uk/pdbsum/1oxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxe 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=1oxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxe OCA], [https://pdbe.org/1oxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oxe RCSB], [https://www.ebi.ac.uk/pdbsum/1oxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxe ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ox/1oxe_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ox/1oxe_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cfp marker plasmid | [[Category: Cfp marker plasmid pWM1009]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Azim | [[Category: Azim MK]] | ||
[[Category: | [[Category: Budisa N]] | ||
[[Category: | [[Category: Holak TA]] | ||
[[Category: | [[Category: Huber R]] | ||
[[Category: | [[Category: Hyun Bae J]] | ||
[[Category: Jung | [[Category: Jung G]] | ||
[[Category: Kim | [[Category: Kim JS]] | ||
[[Category: Moroder | [[Category: Moroder L]] | ||
[[Category: Rubini | [[Category: Rubini M]] | ||
[[Category: Seifert | [[Category: Seifert MH]] | ||
[[Category: Wiegand | [[Category: Wiegand G]] | ||
[[Category: Zumbusch | [[Category: Zumbusch A]] | ||
Latest revision as of 07:47, 17 October 2024
Expansion of the Genetic Code Enables Design of a Novel "Gold" Class of Green Fluorescent ProteinsExpansion of the Genetic Code Enables Design of a Novel "Gold" Class of Green Fluorescent Proteins
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMuch effort has been dedicated to the design of significantly red shifted variants of the green fluorescent protein (GFP) from Aequoria victora (av). These approaches have been based on classical engineering with the 20 canonical amino acids. We report here an expansion of these efforts by incorporation of an amino substituted variant of tryptophan into the "cyan" GFP mutant, which turned it into a "gold" variant. This variant possesses a red shift in emission unprecedented for any avFP, similar to "red" FPs, but with enhanced stability and a very low aggregation tendency. An increasing number of non-natural amino acids are available for chromophore redesign (by engineering of the genetic code) and enable new general strategies to generate novel classes of tailor-made GFP proteins. Expansion of the genetic code enables design of a novel "gold" class of green fluorescent proteins.,Bae JH, Rubini M, Jung G, Wiegand G, Seifert MH, Azim MK, Kim JS, Zumbusch A, Holak TA, Moroder L, Huber R, Budisa N J Mol Biol. 2003 May 16;328(5):1071-81. PMID:12729742[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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