3pjb: Difference between revisions
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<StructureSection load='3pjb' size='340' side='right'caption='[[3pjb]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='3pjb' size='340' side='right'caption='[[3pjb]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3pjb]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3pjb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bubble-tip_anemone Bubble-tip anemone]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PJB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PJB 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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=NRQ:{(4Z)-4-(4-HYDROXYBENZYLIDENE)-2-[3-(METHYLTHIO)PROPANIMIDOYL]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>NRQ</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NRQ:{(4Z)-4-(4-HYDROXYBENZYLIDENE)-2-[3-(METHYLTHIO)PROPANIMIDOYL]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>NRQ</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bx9|3bx9]], [[3bxa|3bxa]], [[3bxb|3bxb]], [[3bxc|3bxc]], [[3pib|3pib]], [[3pj5|3pj5]], [[3pj7|3pj7]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bx9|3bx9]], [[3bxa|3bxa]], [[3bxb|3bxb]], [[3bxc|3bxc]], [[3pib|3pib]], [[3pj5|3pj5]], [[3pj7|3pj7]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pjb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pjb OCA], [https://pdbe.org/3pjb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pjb RCSB], [https://www.ebi.ac.uk/pdbsum/3pjb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pjb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 11:41, 25 May 2022
Crystal structure of red fluorescent protein eqFP578 crystallized at pH 4.0Crystal structure of red fluorescent protein eqFP578 crystallized at pH 4.0
Structural highlights
Publication Abstract from PubMedThe wild type red fluorescent protein eqFP578 (from sea anemone Entacmaea quadricolor, lambdaex = 552 nm, lambdaem = 578 nm) and its bright far-red fluorescent variant Katushka (lambdaex = 588 nm, lambdaem = 635 nm) are characterized by the pronounced pH dependence of their fluorescence. The crystal structures of eqFP578f (eqFP578 with two point mutations improving the protein folding) and Katushka have been determined at the resolution ranging from 1.15 to 1.85 A at two pH values, corresponding to low and high level of fluorescence. The observed extinguishing of fluorescence upon reducing pH in eqFP578f and Katushka has been shown to be accompanied by the opposite trans-cis and cis-trans chromophore isomerization, respectively. Asn143, Ser158, His197 and Ser143, Leu174, and Arg197 have been shown to stabilize the respective trans and cis fluorescent states of the chromophores in eqFP578f and Katushka at higher pH. The cis state has been suggested as being primarily responsible for the observed far-red shift of the emission maximum of Katushka relative to that of eqFP578f. Crystallographic study of red fluorescent protein eqFP578 and its far-red variant Katushka reveals opposite pH-induced isomerization of chromophore.,Pletneva NV, Pletnev VZ, Shemiakina II, Chudakov DM, Artemyev I, Wlodawer A, Dauter Z, Pletnev S Protein Sci. 2011 May 11. doi: 10.1002/pro.654. PMID:21563226[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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