1myw
From Proteopedia
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| - | [[Image:1myw.png|left|200px]] | ||
| - | + | ==CRYSTAL STRUCTURE OF A YELLOW FLUORESCENT PROTEIN WITH IMPROVED MATURATION AND REDUCED ENVIRONMENTAL SENSITIVITY== | |
| + | <StructureSection load='1myw' size='340' side='right'caption='[[1myw]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1myw]] 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=1MYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MYW 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]] 2.2Å</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=1myw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myw OCA], [https://pdbe.org/1myw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1myw RCSB], [https://www.ebi.ac.uk/pdbsum/1myw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1myw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/my/1myw_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1myw ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Yellow emission variants of green fluorescent protein (GFP) have been found useful in a variety of applications in biological systems due to their red-shifted emission spectrum and sensitivity to environmental parameters, such as pH and ionic strength. However, slow maturation properties and new requirements for more intense fluorescence necessitated further mutagenesis studies of these proteins. Venus, a new variant with improved maturation and brightness, as well as reduced environmental dependence, was recently developed by introducing five mutations into the well characterized variant, enhanced yellow fluorescent protein (EYFP). In this paper, we present the crystal structure of Venus at 2.2 A resolution, which enabled us to correlate its novel features with these mutation points. The rearrangement of several side chains near the chromophore, initiated by the F46L mutation, was found to improve maturation at 37 degrees C by removing steric and energetic constraints, which may hinder folding of the polypeptide chain, and by accelerating the oxidation of the Calpha-Cbeta bond of Tyr(66) during chromophore formation. M153T, V163A, and S175G were also found to improve the rate of maturation by creating regions of greater flexibility. F64L induced large conformational changes in the molecule, leading to the removal of halide sensitivity by preventing ion access to the binding site. | ||
| - | + | Crystal structure of venus, a yellow fluorescent protein with improved maturation and reduced environmental sensitivity.,Rekas A, Alattia JR, Nagai T, Miyawaki A, Ikura M J Biol Chem. 2002 Dec 27;277(52):50573-8. Epub 2002 Oct 4. PMID:12370172<ref>PMID:12370172</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1myw" style="background-color:#fffaf0;"></div> | |
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==See Also== | ==See Also== | ||
| - | + | *[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |
| - | + | == References == | |
| - | *[[Green Fluorescent Protein|Green Fluorescent Protein]] | + | <references/> |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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| - | == | + | |
| - | < | + | |
[[Category: Aequorea victoria]] | [[Category: Aequorea victoria]] | ||
| - | [[Category: Alattia | + | [[Category: Large Structures]] |
| - | [[Category: Ikura | + | [[Category: Alattia JR]] |
| - | [[Category: Miyawaki | + | [[Category: Ikura M]] |
| - | [[Category: Nagai | + | [[Category: Miyawaki A]] |
| - | [[Category: Rekas | + | [[Category: Nagai T]] |
| - | + | [[Category: Rekas A]] | |
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Current revision
CRYSTAL STRUCTURE OF A YELLOW FLUORESCENT PROTEIN WITH IMPROVED MATURATION AND REDUCED ENVIRONMENTAL SENSITIVITY
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