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| | <StructureSection load='1s6z' size='340' side='right'caption='[[1s6z]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='1s6z' size='340' side='right'caption='[[1s6z]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1s6z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S6Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1s6z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S6Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 1.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CR0:[2-(1-AMINO-2-HYDROXYPROPYL)-2-HYDROXY-4-ISOBUTYL-5-OXO-2,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETALDEHYDE'>CR0</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CR0:[2-(1-AMINO-2-HYDROXYPROPYL)-2-HYDROXY-4-ISOBUTYL-5-OXO-2,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETALDEHYDE'>CR0</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;'>[[1emg|1emg]], [[1rm9|1rm9]], [[1rmo|1rmo]], [[1rmp|1rmp]], [[1qyf|1qyf]]</div></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=1s6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s6z OCA], [https://pdbe.org/1s6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s6z RCSB], [https://www.ebi.ac.uk/pdbsum/1s6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s6z 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=1s6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s6z OCA], [https://pdbe.org/1s6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s6z RCSB], [https://www.ebi.ac.uk/pdbsum/1s6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s6z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == 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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Synthetic construct sequences]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Huffman, H A]] | + | [[Category: Huffman HA]] |
| - | [[Category: Phail, M E]] | + | [[Category: Phail ME]] |
| - | [[Category: Rosenow, M A]] | + | [[Category: Rosenow MA]] |
| - | [[Category: Wachter, R M]] | + | [[Category: Wachter RM]] |
| - | [[Category: Backbone cyclization]]
| + | |
| - | [[Category: Chromophore]]
| + | |
| - | [[Category: Eleven-stranded beta barrel]]
| + | |
| - | [[Category: Gfp-like protein]]
| + | |
| - | [[Category: Luminescent protein]]
| + | |
| - | [[Category: Trapped intermediate]]
| + | |
| 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 colorless variant of green fluorescent protein (GFP) containing the Y66L substitution has been determined to 1.5 A. Crystallographic evidence is presented for the formation of a trapped intermediate on the pathway of chromophore maturation, where the peptide backbone of residues 65-67 has condensed to form a five-membered heterocyclic ring. The hydroxyl leaving group remains attached to the ring as confirmed by high-resolution electrospray mass spectrometry. The alpha-carbon of residue 66 exhibits trigonal planar geometry, consistent with ring oxidation by molecular oxygen. Side chain positions of surrounding residues are not perturbed, in contrast to structural results obtained for the GFPsol-S65G/Y66G variant [Barondeau, D. P., Putnam, C. D., Kassmann, C. J., Tainer, J. A., and Getzoff, E. D. (2003) Proc. Natl. Acad. Sci. U.S.A. 100, 12111-12116]. The data are in accord with a reaction pathway in which dehydration is the last of three chemical steps in GFP chromophore formation. A novel mechanism for chromophore biosynthesis is proposed: when the protein folds, the backbone condenses to form a cyclopentyl tetrahedral intermediate. In the second step, the ring is oxidized by molecular oxygen. In the third and final step, elimination of the hydroxyl leaving group as water is coupled to a proton transfer reaction that may proceed via hydrogen-bonded solvent molecules. Replacement of the aromatic Tyr66 with an aliphatic residue appears to have a profound effect on the efficiency of ring dehydration. The proposed mechanism has important implications for understanding the factors that limit the maturation rate of GFP.
The crystal structure of the Y66L variant of green fluorescent protein supports a cyclization-oxidation-dehydration mechanism for chromophore maturation.,Rosenow MA, Huffman HA, Phail ME, Wachter RM Biochemistry. 2004 Apr 20;43(15):4464-72. PMID:15078092[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rosenow MA, Huffman HA, Phail ME, Wachter RM. The crystal structure of the Y66L variant of green fluorescent protein supports a cyclization-oxidation-dehydration mechanism for chromophore maturation. Biochemistry. 2004 Apr 20;43(15):4464-72. PMID:15078092 doi:10.1021/bi0361315
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