|
|
| Line 3: |
Line 3: |
| | <StructureSection load='7a8c' size='340' side='right'caption='[[7a8c]], [[Resolution|resolution]] 2.13Å' scene=''> | | <StructureSection load='7a8c' size='340' side='right'caption='[[7a8c]], [[Resolution|resolution]] 2.13Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7a8c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeqvi Aeqvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A8C FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A8C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 2.13Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4xow|4xow]], [[4xov|4xov]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gfp ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 AEQVI])</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=7a8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a8c OCA], [https://pdbe.org/7a8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a8c RCSB], [https://www.ebi.ac.uk/pdbsum/7a8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a8c 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=7a8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a8c OCA], [https://pdbe.org/7a8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a8c RCSB], [https://www.ebi.ac.uk/pdbsum/7a8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a8c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| Line 19: |
Line 17: |
| | </div> | | </div> |
| | <div class="pdbe-citations 7a8c" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 7a8c" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aeqvi]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dedecker, P]] | + | [[Category: De Zitter E]] |
| - | [[Category: Meervelt, L Van]]
| + | [[Category: Dedecker P]] |
| - | [[Category: Zitter, E De]]
| + | [[Category: Van Meervelt L]] |
| - | [[Category: Fluorescent protein]] | + | |
| - | [[Category: Reversible photoswitchable fluorescent protein]] | + | |
| Structural highlights
Publication Abstract from PubMed
Anisotropic environments can drastically alter the spectroscopy and photochemistry of molecules, leading to complex structure-function relationships. We examined this using fluorescent proteins as easy-to-modify model systems. Starting from a single scaffold, we have developed a range of 27 photochromic fluorescent proteins that cover a broad range of spectroscopic properties, including the determination of 43 crystal structures. Correlation and principal component analysis confirmed the complex relationship between structure and spectroscopy, but also allowed us to identify consistent trends and to relate these to the spatial organization. We find that changes in spectroscopic properties can come about through multiple underlying mechanisms, of which polarity, hydrogen bonding and presence of water molecules are key modulators. We anticipate that our findings and rich structure/spectroscopy dataset can open opportunities for the development and evaluation of new and existing protein engineering methods.
Structure-Function Dataset Reveals Environment Effects within a Fluorescent Protein Model System.,De Zitter E, Hugelier S, Duwe S, Vandenberg W, Tebo AG, Van Meervelt L, Dedecker P Angew Chem Int Ed Engl. 2021 Feb 4. doi: 10.1002/anie.202015201. PMID:33543524[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ De Zitter E, Hugelier S, Duwe S, Vandenberg W, Tebo AG, Van Meervelt L, Dedecker P. Structure-Function Dataset Reveals Environment Effects within a Fluorescent Protein Model System. Angew Chem Int Ed Engl. 2021 Feb 4. doi: 10.1002/anie.202015201. PMID:33543524 doi:http://dx.doi.org/10.1002/anie.202015201
|
