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1bfp

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BLUE VARIANT OF GREEN FLUORESCENT PROTEIN

Structural highlights

1bfp is a 1 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 2.1Å
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

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.

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

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/1bfp"

Categories: Aequorea victoria | Large Structures | Remington SJ | Wachter RM

@@ Line 3: / Line 3: @@
 <StructureSection load='1bfp' size='340' side='right'caption='[[1bfp]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bfp]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/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]] 2.1&#8491;</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=1bfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfp OCA], [http://pdbe.org/1bfp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bfp RCSB], [http://www.ebi.ac.uk/pdbsum/1bfp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bfp ProSAT]</span></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>
 </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 30: / Line 31: @@
 ==See Also==
-*[[Green Fluorescent Protein|Green Fluorescent Protein]]
+*[[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: Aequorea victoria]]
 [[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]]

1bfp

From Proteopedia

Current revision

BLUE VARIANT OF GREEN FLUORESCENT PROTEIN

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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