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| | ==Fluorescent protein from Acropora digitifera== | | ==Fluorescent protein from Acropora digitifera== |
| - | <StructureSection load='6aa7' size='340' side='right' caption='[[6aa7]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='6aa7' size='340' side='right'caption='[[6aa7]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6aa7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acrdi Acrdi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AA7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6aa7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acropora_digitifera Acropora digitifera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AA7 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=XYG:[(4Z)-2-[(1Z)-ETHANIMIDOYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>XYG</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]] 1.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">M, LWE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70779 ACRDI])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XYG:[(4Z)-2-[(1Z)-ETHANIMIDOYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>XYG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6aa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aa7 OCA], [http://pdbe.org/6aa7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aa7 RCSB], [http://www.ebi.ac.uk/pdbsum/6aa7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aa7 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=6aa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aa7 OCA], [https://pdbe.org/6aa7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6aa7 RCSB], [https://www.ebi.ac.uk/pdbsum/6aa7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6aa7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A1S7IWI8_ACRDI A0A1S7IWI8_ACRDI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acrdi]] | |
| - | [[Category: Hwang, K Y]] | |
| - | [[Category: Kim, S E]] | |
| - | [[Category: Nam, K H]] | |
| | [[Category: Acropora digitifera]] | | [[Category: Acropora digitifera]] |
| - | [[Category: Chromophore]] | + | [[Category: Large Structures]] |
| - | [[Category: Fluorescent protein]] | + | [[Category: Hwang KY]] |
| - | [[Category: Red fluorescent protein]] | + | [[Category: Kim SE]] |
| | + | [[Category: Nam KH]] |
| Structural highlights
Function
A0A1S7IWI8_ACRDI
Publication Abstract from PubMed
Fluorescent proteins (FPs) possess a wide variety of spectral properties that make them of widespread interest as optical markers. These proteins can be applied as pH indicators or metal biosensors. The discovery and characterization of new fluorescent proteins is expected to further extend their application. Here, we report the spectral and structural analysis of a red fluorescent protein from Acropora digitifera (designated AdRed). This protein shows a tetrameric state and is red emitting, with excitation and emission maxima at 567 and 612 nm, respectively. Its crystal structure shows the tetrameric interface stabilized by hydrogen bonding and salt bridges. The electron density map of the chromophore, consisting of Asp66-Tyr67-Gly68, shows the decarboxylated side chain of Asp66. Ser223, located near the chromophore, has the role of bridging His202 and Glu221, and is part of the hydrogen bond network. Mutated AdRed with Cys148Ser reveals a blue shift in fluorescence excitation and emission. Our results provide insights into understanding the molecular function of AdRed and other FPs.
Spectral and structural analysis of a red fluorescent protein from Acropora digitifera.,Kim SE, Hwang KY, Nam KH Protein Sci. 2019 Feb;28(2):375-381. doi: 10.1002/pro.3540. Epub 2018 Nov 27. PMID:30368951[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim SE, Hwang KY, Nam KH. Spectral and structural analysis of a red fluorescent protein from Acropora digitifera. Protein Sci. 2019 Feb;28(2):375-381. doi: 10.1002/pro.3540. Epub 2018 Nov 27. PMID:30368951 doi:http://dx.doi.org/10.1002/pro.3540
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