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| | <StructureSection load='6qqa' size='340' side='right'caption='[[6qqa]], [[Resolution|resolution]] 1.66Å' scene=''> | | <StructureSection load='6qqa' size='340' side='right'caption='[[6qqa]], [[Resolution|resolution]] 1.66Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6qqa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeqvi Aeqvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QQA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QQA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6qqa]] 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=6QQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QQA FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRF:[(4Z)-2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(1H-INDOL-3-YLMETHYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>CRF</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]] 1.66Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GFP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 AEQVI])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRF:[(4Z)-2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(1H-INDOL-3-YLMETHYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>CRF</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=6qqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qqa OCA], [http://pdbe.org/6qqa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qqa RCSB], [http://www.ebi.ac.uk/pdbsum/6qqa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qqa 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=6qqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qqa OCA], [https://pdbe.org/6qqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qqa RCSB], [https://www.ebi.ac.uk/pdbsum/6qqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qqa ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI]] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. | + | [https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. |
| | <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: Aeqvi]] | + | [[Category: Aequorea victoria]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aumonier, S]] | + | [[Category: Aumonier S]] |
| - | [[Category: Gotthard, G]] | + | [[Category: Gotthard G]] |
| - | [[Category: Royant, A]] | + | [[Category: Royant A]] |
| - | [[Category: Cerulean]]
| + | |
| - | [[Category: Fluorescent protein]]
| + | |
| - | [[Category: Hydrogen atom]]
| + | |
| - | [[Category: Room temperature]]
| + | |
| - | [[Category: Tryptophan-based chromophore]]
| + | |
| Structural highlights
Function
GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
Publication Abstract from PubMed
Carrying out macromolecular crystallography (MX) experiments at cryogenic temperatures significantly slows the rate of global radiation damage, thus facilitating the solution of high-resolution crystal structures of macromolecules. However, cryo-MX experiments suffer from the early onset of so-called specific radiation damage that affects certain amino-acid residues and, in particular, the active sites of many proteins. Here, a series of MX experiments are described which suggest that specific and global radiation damage are much less decoupled at room temperature than they are at cryogenic temperatures. The results reported here demonstrate the interest in reviving the practice of collecting MX diffraction data at room temperature and allow structural biologists to favourably envisage the development of time-resolved MX experiments at synchrotron sources.
Specific radiation damage is a lesser concern at room temperature.,Gotthard G, Aumonier S, De Sanctis D, Leonard G, von Stetten D, Royant A IUCrJ. 2019 Jun 12;6(Pt 4):665-680. doi: 10.1107/S205225251900616X. eCollection, 2019 Jul 1. PMID:31316810[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gotthard G, Aumonier S, De Sanctis D, Leonard G, von Stetten D, Royant A. Specific radiation damage is a lesser concern at room temperature. IUCrJ. 2019 Jun 12;6(Pt 4):665-680. doi: 10.1107/S205225251900616X. eCollection, 2019 Jul 1. PMID:31316810 doi:http://dx.doi.org/10.1107/S205225251900616X
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