7a7y: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='7a7y' size='340' side='right'caption='[[7a7y]], [[Resolution|resolution]] 0.97Å' scene=''> | <StructureSection load='7a7y' size='340' side='right'caption='[[7a7y]], [[Resolution|resolution]] 0.97Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7a7y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[7a7y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A7Y 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]] 0.97Å</td></tr> | ||
<tr id=' | <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=NO3:NITRATE+ION'>NO3</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=7a7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a7y OCA], [https://pdbe.org/7a7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a7y RCSB], [https://www.ebi.ac.uk/pdbsum/7a7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a7y 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=7a7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a7y OCA], [https://pdbe.org/7a7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a7y RCSB], [https://www.ebi.ac.uk/pdbsum/7a7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a7y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A059PIQ0_AEQVI A0A059PIQ0_AEQVI] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 7a7y" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7a7y" 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: | [[Category: Aequorea victoria]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: De Zitter E]] | ||
[[Category: Dedecker P]] | |||
[[Category: Van Meervelt L]] | |||
[[Category: | |||
[[Category: | |||
Revision as of 15:05, 1 February 2024
rsGreen0.7-F145Q in the green-on statersGreen0.7-F145Q in the green-on state
Structural highlights
FunctionPublication Abstract from PubMedAnisotropic 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 AlsoReferences
|
| ||||||||||||||||||