1oxe: Difference between revisions

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<StructureSection load='1oxe' size='340' side='right'caption='[[1oxe]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
<StructureSection load='1oxe' size='340' side='right'caption='[[1oxe]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1emb|1emb]]</div></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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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oxe ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oxe ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Much 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<ref>PMID:12729742</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1oxe" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cfp marker plasmid pwm1009]]
[[Category: Cfp marker plasmid pWM1009]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Azim, M K]]
[[Category: Azim MK]]
[[Category: Bae, J Hyun]]
[[Category: Budisa N]]
[[Category: Budisa, N]]
[[Category: Holak TA]]
[[Category: Holak, T A]]
[[Category: Huber R]]
[[Category: Huber, R]]
[[Category: Hyun Bae J]]
[[Category: Jung, G]]
[[Category: Jung G]]
[[Category: Kim, J S]]
[[Category: Kim JS]]
[[Category: Moroder, L]]
[[Category: Moroder L]]
[[Category: Rubini, M]]
[[Category: Rubini M]]
[[Category: Seifert, M H]]
[[Category: Seifert MH]]
[[Category: Wiegand, G]]
[[Category: Wiegand G]]
[[Category: Zumbusch, A]]
[[Category: Zumbusch A]]
[[Category: Amino acid incorporation]]
[[Category: Chromophore]]
[[Category: Genetic code]]
[[Category: Green fluorescent protein]]
[[Category: Luminescent protein]]
[[Category: Tryptophan]]

Revision as of 08:51, 17 April 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

1oxe is a 1 chain structure with sequence from Cfp marker plasmid pWM1009. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.15Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1oxe, resolution 1.15Å

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OCA
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