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| | <StructureSection load='3gl4' size='340' side='right'caption='[[3gl4]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='3gl4' size='340' side='right'caption='[[3gl4]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3gl4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anthomedusae_sp._dc-2005 Anthomedusae sp. dc-2005]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GL4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3GL4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3gl4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anthomedusae_sp._DC-2005 Anthomedusae sp. DC-2005]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GL4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GL4 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRQ:[2-(3-CARBAMOYL-1-IMINO-PROPYL)-4-(4-HYDROXY-BENZYLIDENE)-5-OXO-4,5-DIHYDRO-IMIDAZOL-1-YL]-ACETIC+ACID'>CRQ</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gb3|3gb3]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRQ:[2-(3-CARBAMOYL-1-IMINO-PROPYL)-4-(4-HYDROXY-BENZYLIDENE)-5-OXO-4,5-DIHYDRO-IMIDAZOL-1-YL]-ACETIC+ACID'>CRQ</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3gl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gl4 OCA], [http://pdbe.org/3gl4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gl4 RCSB], [http://www.ebi.ac.uk/pdbsum/3gl4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gl4 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=3gl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gl4 OCA], [https://pdbe.org/3gl4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gl4 RCSB], [https://www.ebi.ac.uk/pdbsum/3gl4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gl4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q2TCH5_9CNID Q2TCH5_9CNID] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anthomedusae sp. dc-2005]] | + | [[Category: Anthomedusae sp. DC-2005]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pletnev, S]] | + | [[Category: Pletnev S]] |
| - | [[Category: Pletnev, V Z]] | + | [[Category: Pletnev VZ]] |
| - | [[Category: Pletneva, N V]] | + | [[Category: Pletneva NV]] |
| - | [[Category: Fluorescent protein]]
| + | |
| - | [[Category: Genetically encoded photosensitizer]]
| + | |
| - | [[Category: Killerred]]
| + | |
| - | [[Category: Phototoxicity]]
| + | |
| Structural highlights
Function
Q2TCH5_9CNID
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 PubMed
KillerRed is the only known fluorescent protein that demonstrates notable phototoxicity, exceeding that of the other green and red fluorescent proteins by at least 1,000-fold. KillerRed could serve as an instrument to inactivate target proteins or to kill cell populations in photodynamic therapy. However, the nature of KillerRed phototoxicity has remained unclear, impeding the development of more phototoxic variants. Here we present the results of a high resolution crystallographic study of KillerRed in the active fluorescent and in the photobleached non-fluorescent states. A unique and striking feature of the structure is a water-filled channel reaching the chromophore area from the end cap of the beta-barrel that is probably one of the key structural features responsible for phototoxicity. A study of the structure-function relationship of KillerRed, supported by structure-based, site-directed mutagenesis, has also revealed the key residues most likely responsible for the phototoxic effect. In particular, Glu(68) and Ser(119), located adjacent to the chromophore, have been assigned as the primary trigger of the reaction chain.
Structural basis for phototoxicity of the genetically encoded photosensitizer KillerRed.,Pletnev S, Gurskaya NG, Pletneva NV, Lukyanov KA, Chudakov DM, Martynov VI, Popov VO, Kovalchuk MV, Wlodawer A, Dauter Z, Pletnev V J Biol Chem. 2009 Nov 13;284(46):32028-39. Epub 2009 Sep 8. PMID:19737938[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pletnev S, Gurskaya NG, Pletneva NV, Lukyanov KA, Chudakov DM, Martynov VI, Popov VO, Kovalchuk MV, Wlodawer A, Dauter Z, Pletnev V. Structural basis for phototoxicity of the genetically encoded photosensitizer KillerRed. J Biol Chem. 2009 Nov 13;284(46):32028-39. Epub 2009 Sep 8. PMID:19737938 doi:10.1074/jbc.M109.054973
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