3lvd
From Proteopedia
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| - | [[ | + | ==Crystal structure of GFP-like protein aceGFP_G222E (A. coerulescens). UV-photoconverted green form.== |
| + | <StructureSection load='3lvd' size='340' side='right' caption='[[3lvd]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3lvd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aequorea_coerulescens Aequorea coerulescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LVD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LVD FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GYS:[(4Z)-2-(1-AMINO-2-HYDROXYETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYS</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lva|3lva]], [[3lvc|3lvc]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lvd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lvd RCSB], [http://www.ebi.ac.uk/pdbsum/3lvd PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/lv/3lvd_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The acGFPL is the first-identified member of a novel, colorless and non-fluorescent group of green fluorescent protein (GFP)-like proteins. Its mutant aceGFP, with Gly replacing the invariant catalytic Glu-222, demonstrates a relatively fast maturation rate and bright green fluorescence (lambda(ex) = 480 nm, lambda(em) = 505 nm). The reverse G222E single mutation in aceGFP results in the immature, colorless variant aceGFP-G222E, which undergoes irreversible photoconversion to a green fluorescent state under UV light exposure. Here we present a high resolution crystallographic study of aceGFP and aceGFP-G222E in the immature and UV-photoconverted states. A unique and striking feature of the colorless aceGFP-G222E structure is the chromophore in the trapped intermediate state, where cyclization of the protein backbone has occurred, but Tyr-66 still stays in the native, non-oxidized form, with C(alpha) and C(beta) atoms in the sp(3) hybridization. This experimentally observed immature aceGFP-G222E structure, characterized by the non-coplanar arrangement of the imidazolone and phenolic rings, has been attributed to one of the intermediate states in the GFP chromophore biosynthesis. The UV irradiation (lambda = 250-300 nm) of aceGFP-G222E drives the chromophore maturation further to a green fluorescent state, characterized by the conventional coplanar bicyclic structure with the oxidized double Tyr-66 C(alpha)=C(beta) bond and the conjugated system of pi-electrons. Structure-based site-directed mutagenesis has revealed a critical role of the proximal Tyr-220 in the observed effects. In particular, an alternative reaction pathway via Tyr-220 rather than conventional wild type Glu-222 has been proposed for aceGFP maturation. | ||
| - | + | Structural evidence for a dehydrated intermediate in green fluorescent protein chromophore biosynthesis.,Pletneva NV, Pletnev VZ, Lukyanov KA, Gurskaya NG, Goryacheva EA, Martynov VI, Wlodawer A, Dauter Z, Pletnev S J Biol Chem. 2010 May 21;285(21):15978-84. Epub 2010 Mar 9. PMID:20220148<ref>PMID:20220148</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
| - | *[[Alyssa Marsico/Sandbox 1|Alyssa Marsico/Sandbox 1]] | ||
| - | *[[Devon McCarthy/Sandbox 1|Devon McCarthy/Sandbox 1]] | ||
*[[Green Fluorescent Protein|Green Fluorescent Protein]] | *[[Green Fluorescent Protein|Green Fluorescent Protein]] | ||
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | == | + | </StructureSection> |
| - | < | + | |
[[Category: Aequorea coerulescens]] | [[Category: Aequorea coerulescens]] | ||
| - | [[Category: Pletnev, S V | + | [[Category: Pletnev, S V]] |
| - | [[Category: Pletnev, V Z | + | [[Category: Pletnev, V Z]] |
| - | [[Category: Pletneva, N V | + | [[Category: Pletneva, N V]] |
[[Category: Chromophore biosynthesis]] | [[Category: Chromophore biosynthesis]] | ||
[[Category: Colorless gfp-like protein]] | [[Category: Colorless gfp-like protein]] | ||
[[Category: Fluorescent protein]] | [[Category: Fluorescent protein]] | ||
[[Category: Green fluorescent protein]] | [[Category: Green fluorescent protein]] | ||
Revision as of 18:27, 21 December 2014
Crystal structure of GFP-like protein aceGFP_G222E (A. coerulescens). UV-photoconverted green form.
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