2duf: Difference between revisions

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-[[Image:2duf.jpg|left|200px]]
-<!--
+==crystal structure of a green fluorescent protein variant S65T/H148D at pH 5.6==
-The line below this paragraph, containing "STRUCTURE_2duf", creates the "Structure Box" on the page.
+<StructureSection load='2duf' size='340' side='right'caption='[[2duf]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2duf]] 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=2DUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DUF FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C12:2-(1-AMINO-2-HYDROXYPROPYL)-4-(4-HYDROXYBENZYL)-1-(2-OXOETHYL)-1H-IMIDAZOL-5-OLATE'>C12</scene></td></tr>
-{{STRUCTURE_2duf|  PDB=2duf  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2duf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2duf OCA], [https://pdbe.org/2duf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2duf RCSB], [https://www.ebi.ac.uk/pdbsum/2duf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2duf 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/du/2duf_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=2duf ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Wild type green fluorescent protein (wt-GFP) and the variant S65T/H148D each exhibit two absorption bands, A and B, which are associated with the protonated and deprotonated chromophores, respectively. Excitation of either band leads to green emission. In wt-GFP, excitation of band A ( approximately 395 nm) leads to green emission with a rise time of 10-15 ps, due to excited-state proton transfer (ESPT) from the chromophore hydroxyl group to an acceptor. This process produces an anionic excited-state intermediate I* that subsequently emits a green photon. In the variant S65T/H148D, the A band absorbance maximum is red-shifted to approximately 415 nm, and as detailed in the accompanying papers, when the A band is excited, green fluorescence appears with a rise time shorter than the instrument time resolution ( approximately 170 fs). On the basis of the steady-state spectroscopy and high-resolution crystal structures of several variants described herein, it is proposed that in S65T/H148D, the red shift of absorption band A and the ultrafast appearance of green fluorescence upon excitation of band A are due to a very short (&lt;or=2.4 A), and possibly low-barrier, hydrogen bond between the chromophore hydroxyl and introduced Asp148.
-'''crystal structure of a green fluorescent protein variant S65T/H148D at pH 5.6'''
+Ultrafast excited-state dynamics in the green fluorescent protein variant S65T/H148D. 1. Mutagenesis and structural studies.,Shu X, Kallio K, Shi X, Abbyad P, Kanchanawong P, Childs W, Boxer SG, Remington SJ Biochemistry. 2007 Oct 30;46(43):12005-13. Epub 2007 Oct 6. PMID:17918959<ref>PMID:17918959</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2duf" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-DUF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DUF OCA].
+*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Aequorea victoria]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Remington, S J.]]
+[[Category: Remington SJ]]
-[[Category: Shu, X.]]
+[[Category: Shu X]]
-[[Category: Excited state proton transfer]]
-[[Category: Green fluorescent protein]]
-[[Category: Very short hydrogen bond]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 01:24:01 2008''