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| | <StructureSection load='1bfp' size='340' side='right'caption='[[1bfp]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1bfp' size='340' side='right'caption='[[1bfp]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1bfp]] 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=1BFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BFP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bfp]] 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=1BFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BFP FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IIC:4-IMIDAZOLMETHYLENE-5-IMIDAZOLONE+CHROMOPHORE'>IIC</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]] 2.1Å</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IIC:4-IMIDAZOLMETHYLENE-5-IMIDAZOLONE+CHROMOPHORE'>IIC</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=1bfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfp OCA], [https://pdbe.org/1bfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bfp RCSB], [https://www.ebi.ac.uk/pdbsum/1bfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bfp 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=1bfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfp OCA], [https://pdbe.org/1bfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bfp RCSB], [https://www.ebi.ac.uk/pdbsum/1bfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bfp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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.
| + | [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. |
| | == 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: Aeqvi]] | + | [[Category: Aequorea victoria]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Remington, S J]] | + | [[Category: Remington SJ]] |
| - | [[Category: Wachter, R M]] | + | [[Category: Wachter RM]] |
| - | [[Category: Bioluminescense]]
| + | |
| - | [[Category: Blue emission]]
| + | |
| - | [[Category: Fluorescent protein]]
| + | |
| - | [[Category: Fluorophore]]
| + | |
| - | [[Category: Luminescence]]
| + | |
| - | [[Category: Mutant]]
| + | |
| 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.
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
The crystal structure of a blue emission variant (Y66H/Y145F) of the Aequorea victoria green fluorescent protein has been determined by molecular replacement and the model refined. The crystallographic R-factor is 18.1% for all data from 20 to 2.1 A, and the model geometry is excellent. The chromophore is non-native and is autocatalytically generated from the internal tripeptide Ser65-His66-Gly67. The final electron density maps indicate that the formation of the chromophore is complete, including 1,2 dehydration of His66 as indicated by the planarity of the chromophore. The chromophore is in the cis conformation, with no evidence for any substantial fraction of the trans configuration or uncyclized apoprotein, and is well-shielded from bulk solvent by the folded protein. These characteristics indicate that the machinery for production of the chromophore from a buried tripeptide unit is not only intact but also highly efficient in spite of a major change in chromophore chemical structure. Nevertheless, there are significant rearrangements in the hydrogen bond configuration around the chromophore as compared to wild-type, indicating flexibility of the active site. pH titration of the intact protein and the chromopeptide (pKa1 = 4.9 +/- 0.1, pKa2 = 12.0 +/- 0.1) suggests that the predominant form of the chromophore in the intact protein is electrically neutral. In contrast to the wild-type protein [Chattoraj, M., King, B. A., Bublitz, G. U., & Boxer, S. G. (1996) Proc. Natl. Acad. Sci. U.S.A., 8362-8367], femtosecond fluorescence up-conversion spectroscopy of the intact protein and a partially deuterated form strongly suggests that excited-state proton transfer is not coupled to fluorescence emission.
Crystal structure and photodynamic behavior of the blue emission variant Y66H/Y145F of green fluorescent protein.,Wachter RM, King BA, Heim R, Kallio K, Tsien RY, Boxer SG, Remington SJ Biochemistry. 1997 Aug 12;36(32):9759-65. PMID:9245407[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wachter RM, King BA, Heim R, Kallio K, Tsien RY, Boxer SG, Remington SJ. Crystal structure and photodynamic behavior of the blue emission variant Y66H/Y145F of green fluorescent protein. Biochemistry. 1997 Aug 12;36(32):9759-65. PMID:9245407 doi:10.1021/bi970563w
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