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| | <StructureSection load='1kp5' size='340' side='right'caption='[[1kp5]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='1kp5' size='340' side='right'caption='[[1kp5]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kp5]] is a 2 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=1KP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KP5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kp5]] is a 2 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=1KP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KP5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.6Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GYS:[(4Z)-2-(1-AMINO-2-HYDROXYETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYS</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GYS:[(4Z)-2-(1-AMINO-2-HYDROXYETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1kp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kp5 OCA], [https://pdbe.org/1kp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kp5 RCSB], [https://www.ebi.ac.uk/pdbsum/1kp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kp5 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=1kp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kp5 OCA], [https://pdbe.org/1kp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kp5 RCSB], [https://www.ebi.ac.uk/pdbsum/1kp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kp5 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: Hofmann, A]] | + | [[Category: Hofmann A]] |
| - | [[Category: Iwai, H]] | + | [[Category: Iwai H]] |
| - | [[Category: Plueckthun, A]] | + | [[Category: Plueckthun A]] |
| - | [[Category: Wlodawer, A]] | + | [[Category: Wlodawer A]] |
| - | [[Category: Cyclic protein]]
| + | |
| - | [[Category: Cyclised termini]]
| + | |
| - | [[Category: Green fluorescent protein]]
| + | |
| - | [[Category: Luminescent protein]]
| + | |
| 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
Crystals of cyclic green fluorescent protein (cGFP) engineered by the previously reported split intein technology [Iwai et al. (2001), J. Biol. Chem. 276, 16548-16554] were obtained and the structure was solved using molecular replacement. Although the core of the protein can unambiguously be fitted from the first to the last residue of the genuine sequence, the electron density in the region of the linker peptide is rather poor owing to the high water content of the crystals. Therefore, it is concluded that this part of the protein is highly disordered in the present structure and is very flexible. This is supported by the absence of crystal contacts in the linker-peptide region and the fact that the core of the protein exhibits a very similar conformation to that known from other GFP structures, thereby not implicating any constraints arising from the presence of the artificial linker. Nevertheless, the density is consistent with the loop being intact, as confirmed by mass spectroscopy of dissolved crystals. The present structure contains an antiparallel cGFP dimer where the dimer interface is clearly different from other crystal structures featuring two GFP molecules. This adds further support to the fact that the cylinder surface of GFP is rather versatile and can employ various polar and non-polar patches in protein-protein interactions.
Structure of cyclized green fluorescent protein.,Hofmann A, Iwai H, Hess S, Pluckthun A, Wlodawer A Acta Crystallogr D Biol Crystallogr. 2002 Sep;58(Pt 9):1400-6. Epub 2002, Aug 23. PMID:12198295[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hofmann A, Iwai H, Hess S, Pluckthun A, Wlodawer A. Structure of cyclized green fluorescent protein. Acta Crystallogr D Biol Crystallogr. 2002 Sep;58(Pt 9):1400-6. Epub 2002, Aug 23. PMID:12198295 doi:10.1107/S0907444902010454
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