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New page: left|200px<br /><applet load="2a46" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a46, resolution 1.650Å" /> '''Crystal structures ... |
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== | ==Crystal structures of amFP486, a cyan fluorescent protein from Anemonia majano, and variants== | ||
Fluorescent proteins isolated from coral reef organisms can be roughly | <StructureSection load='2a46' size='340' side='right'caption='[[2a46]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2a46]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anemonia_manjano Anemonia manjano]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A46 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]] 1.65Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CR7:[(4Z)-2-[(1S)-1,5-DIAMINOPENTYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>CR7</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=2a46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a46 OCA], [https://pdbe.org/2a46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a46 RCSB], [https://www.ebi.ac.uk/pdbsum/2a46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a46 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GFPL_ANEMA GFPL_ANEMA] Pigment protein that is green in color.<ref>PMID:10504696</ref> | |||
== 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/a4/2a46_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/main_output.php?pdb_ID=2a46 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fluorescent proteins isolated from coral reef organisms can be roughly grouped into four color classes by emission, cyan, green, yellow, and red. To gain insight into the structural basis for cyan emission, the crystal structure of amFP486 (lambda(em)max = 486 nm) was determined by molecular replacement, and the model was refined at 1.65-A resolution. The electron density map reveals a chromophore formed from the tripeptide sequence -K-Y-G- that is indistinguishable from that of GFP (lambda(em)max = 509 nm). However, the chromophore environment closely parallels those of the yellow- and red-shifted homologs zFP538, DsRed, and eqFP611. Mutagenesis was performed for Glu-150, Ala-165, His-199, and Glu-217, which are immediately adjacent to the chromophore. His-199 and Ala-165 are key side chains responsible for the blue shift, presumably by localizing chromophore charge density on the phenolate moiety. Furthermore, in the H199T mutant the fluorescence quantum yield is reduced by a factor of approximately 110. The crystal structures of H199T (lambda(em)max = 515 nm) and E150Q (lambda(em)max = 506 nm) were determined. Remarkably, the H199T structure reveals that the stacking interaction of His-199 with the chromophore also controls the fluorescence efficiency, because the chromophore is statistically distributed in a 1:1 ratio between cis (fluorescent) and trans (nonfluorescent) conformations. | |||
Crystal structures and mutational analysis of amFP486, a cyan fluorescent protein from Anemonia majano.,Henderson JN, Remington SJ Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12712-7. Epub 2005 Aug 24. PMID:16120682<ref>PMID:16120682</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: Anemonia | <div class="pdbe-citations 2a46" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Henderson | <references/> | ||
[[Category: Remington | __TOC__ | ||
</StructureSection> | |||
[[Category: Anemonia manjano]] | |||
[[Category: Large Structures]] | |||
[[Category: Henderson JN]] | |||
[[Category: Remington SJ]] | |||
Latest revision as of 10:18, 23 August 2023
Crystal structures of amFP486, a cyan fluorescent protein from Anemonia majano, and variantsCrystal structures of amFP486, a cyan fluorescent protein from Anemonia majano, and variants
Structural highlights
FunctionGFPL_ANEMA Pigment protein that is green in color.[1] 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 PubMedFluorescent proteins isolated from coral reef organisms can be roughly grouped into four color classes by emission, cyan, green, yellow, and red. To gain insight into the structural basis for cyan emission, the crystal structure of amFP486 (lambda(em)max = 486 nm) was determined by molecular replacement, and the model was refined at 1.65-A resolution. The electron density map reveals a chromophore formed from the tripeptide sequence -K-Y-G- that is indistinguishable from that of GFP (lambda(em)max = 509 nm). However, the chromophore environment closely parallels those of the yellow- and red-shifted homologs zFP538, DsRed, and eqFP611. Mutagenesis was performed for Glu-150, Ala-165, His-199, and Glu-217, which are immediately adjacent to the chromophore. His-199 and Ala-165 are key side chains responsible for the blue shift, presumably by localizing chromophore charge density on the phenolate moiety. Furthermore, in the H199T mutant the fluorescence quantum yield is reduced by a factor of approximately 110. The crystal structures of H199T (lambda(em)max = 515 nm) and E150Q (lambda(em)max = 506 nm) were determined. Remarkably, the H199T structure reveals that the stacking interaction of His-199 with the chromophore also controls the fluorescence efficiency, because the chromophore is statistically distributed in a 1:1 ratio between cis (fluorescent) and trans (nonfluorescent) conformations. Crystal structures and mutational analysis of amFP486, a cyan fluorescent protein from Anemonia majano.,Henderson JN, Remington SJ Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12712-7. Epub 2005 Aug 24. PMID:16120682[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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