5exb: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5exb]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendronephthya_sp. Dendronephthya sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EXB FirstGlance]. <br> | <table><tr><td colspan='2'>[[5exb]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendronephthya_sp. Dendronephthya sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EXB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5SQ:2-[2-[(1~{S})-1-AZANYL-2-(1~{H}-IMIDAZOL-4-YL)ETHYL]-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXIDANYLIDENE-IMIDAZOL-1-YL]ETHANOIC+ACID'>5SQ</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5exb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5exb OCA], [https://pdbe.org/5exb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5exb RCSB], [https://www.ebi.ac.uk/pdbsum/5exb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5exb ProSAT]</span></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=5exb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5exb OCA], [https://pdbe.org/5exb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5exb RCSB], [https://www.ebi.ac.uk/pdbsum/5exb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5exb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8T6U0_9CNID Q8T6U0_9CNID] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Dendronephthya sp]] | [[Category: Dendronephthya sp]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Pletnev | [[Category: Pletnev SV]] | ||
[[Category: Pletnev | [[Category: Pletnev VZ]] | ||
[[Category: Pletneva | [[Category: Pletneva NV]] | ||
Latest revision as of 11:31, 12 July 2023
Wild type green fluorescent protein DendFP (Dendronephthya sp.)Wild type green fluorescent protein DendFP (Dendronephthya sp.)
Structural highlights
FunctionPublication Abstract from PubMedThe fluorescent protein from Dendronephthya sp. (DendFP) is a member of the Kaede-like group of photoconvertible fluorescent proteins with a His62-Tyr63-Gly64 chromophore-forming sequence. Upon irradiation with UV and blue light, the fluorescence of DendFP irreversibly changes from green (506 nm) to red (578 nm). The photoconversion is accompanied by cleavage of the peptide backbone at the C(alpha)-N bond of His62 and the formation of a terminal carboxamide group at the preceding Leu61. The resulting double C(alpha)=C(beta) bond in His62 extends the conjugation of the chromophore pi system to include imidazole, providing the red fluorescence. Here, the three-dimensional structures of native green and photoconverted red forms of DendFP determined at 1.81 and 2.14 A resolution, respectively, are reported. This is the first structure of photoconverted red DendFP to be reported to date. The structure-based mutagenesis of DendFP revealed an important role of positions 142 and 193: replacement of the original Ser142 and His193 caused a moderate red shift in the fluorescence and a considerable increase in the photoconversion rate. It was demonstrated that hydrogen bonding of the chromophore to the Gln116 and Ser105 cluster is crucial for variation of the photoconversion rate. The single replacement Gln116Asn disrupts the hydrogen bonding of Gln116 to the chromophore, resulting in a 30-fold decrease in the photoconversion rate, which was partially restored by a further Ser105Asn replacement. Crystal structure of the fluorescent protein from Dendronephthya sp. in both green and photoconverted red forms.,Pletneva NV, Pletnev S, Pakhomov AA, Chertkova RV, Martynov VI, Muslinkina L, Dauter Z, Pletnev VZ Acta Crystallogr D Struct Biol. 2016 Aug;72(Pt 8):922-32. doi:, 10.1107/S205979831601038X. Epub 2016 Jul 13. PMID:27487823[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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