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1yfp

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STRUCTURE OF YELLOW-EMISSION VARIANT OF GFP

Structural highlights

1yfp is a 2 chain structure with sequence from Aequorea victoria. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

BACKGROUND: Because of its ability to spontaneously generate its own fluorophore, the green fluorescent protein (GFP) from the jellyfish Aequorea victoria is used extensively as a fluorescent marker in molecular and cell biology. The yellow fluorescent proteins (YFPs) have the longest wavelength emissions of all GFP variants examined to date. This shift in the spectrum is the result of a T203Y substitution (single-letter amino acid code), a mutation rationally designed on the basis of the X-ray structure of GFP S65T. RESULTS: We have determined the crystal structures of YFP T203Y/S65G/V68L/S72A and YFP H148G to 2.5 and 2.6 A resolution, respectively. Both structures show clear electron density for nearly coplanar pi-pi stacking between Tyr203 and the chromophore. The chromophore has been displaced by nearly 1 A in comparison to other available structures. Although the H148G mutation results in the generation of a solvent channel to the chromophore cavity, intense fluorescence is maintained. The chromophore in the intact protein can be titrated, and the two variants have pKa values of 7.0 (YFP) and 8.0 (YFP H148G). CONCLUSIONS: The observed red shift of the T203Y YFP variant is proposed to be mainly due to the additional polarizability of the pi-stacked Tyr203. The altered location of the chromophore suggests that the exact positions of nearby residues are not crucial for the chemistry of chromophore formation. The YFPs significantly extend the pH range over which GFPs may be employed as pH indicators in live cells.

Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein.,Wachter RM, Elsliger MA, Kallio K, Hanson GT, Remington SJ Structure. 1998 Oct 15;6(10):1267-77. PMID:9782051^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wachter RM, Elsliger MA, Kallio K, Hanson GT, Remington SJ. Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein. Structure. 1998 Oct 15;6(10):1267-77. PMID:9782051

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yfp"

@@ Line 3: / Line 3: @@
 <StructureSection load='1yfp' size='340' side='right'caption='[[1yfp]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1yfp]] is a 2 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=1YFP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YFP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1yfp]] 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=1YFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YFP FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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></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]] 2.5&#8491;</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=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1yfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yfp OCA], [http://pdbe.org/1yfp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yfp RCSB], [http://www.ebi.ac.uk/pdbsum/1yfp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yfp 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=1yfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yfp OCA], [https://pdbe.org/1yfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yfp RCSB], [https://www.ebi.ac.uk/pdbsum/1yfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yfp ProSAT]</span></td></tr>
 </table>
 == 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 ==See Also==
 *[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
-*[[Green Fluorescent Protein: Research Tool|Green Fluorescent Protein: Research Tool]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Aeqvi]]
+[[Category: Aequorea victoria]]
 [[Category: Large Structures]]
-[[Category: Elsliger, M A]]
+[[Category: Elsliger M-A]]
-[[Category: Hanson, G T]]
+[[Category: Hanson GT]]
-[[Category: Kallio, K]]
+[[Category: Kallio K]]
-[[Category: Remington, S J]]
+[[Category: Remington SJ]]
-[[Category: Wachter, R M]]
+[[Category: Wachter RM]]
-[[Category: Bioluminescence]]
-[[Category: Fluorescent tag]]
-[[Category: Green fluorescent protein]]
-[[Category: Luminescence]]
-[[Category: Photoactive protein]]
-[[Category: Yellow-emission variant]]

1yfp

From Proteopedia

Current revision

STRUCTURE OF YELLOW-EMISSION VARIANT OF GFP

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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