4eul - Revision history

OCA at 06:56, 27 November 2024

2024-11-27T06:56:58Z

← Older revision		Revision as of 06:56, 27 November 2024
Line 10:		Line 10:
	== 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.
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Enhanced Green Fluorescent Protein (EGFP) is one of the most widely used engineered variants of the original wild-type Green Fluorescent Protein. Here, we report the high resolution (1.35 A) structure of EGFP crystallised in its untagged sequence form that reveals the combined impact of the F64L and S65T, that give rise to improved folding and spectral characteristics. The overall structure of EGFP is very similar to wt GFP, forming the classical beta-barrel fold with the chromophore containing helix running through the core of the structure. Replacement of Phe64 with Leu in EGFP results in subtle rearrangement of hydrophobic core packing close to the chromophore including the reduction in surface exposure of two hydrophobic residues. Replacement of Ser65 with Thr has a significant impact on the local hydrogen bond network in the vicinity of the chromophore. Detailed analysis of electron density reveals that several residues close to the chromophore occupy at least two distinct conformations. This includes Glu222 that defines the charged state on the chromophore, with the two conformations having slightly different effects on the hydrogen bond network surrounding the chromophore. Hence, the reported high-resolution structure of EGFP has provided a long overdue molecular description of one of the most important fluorescent protein variants currently in general use.

			Crystal structure of enhanced green fluorescent protein to 1.35 A resolution reveals alternative conformations for Glu222.,Arpino JA, Rizkallah PJ, Jones DD PLoS One. 2012;7(10):e47132. doi: 10.1371/journal.pone.0047132. Epub 2012 Oct 16. PMID:23077555<ref>PMID:23077555</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 4eul" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Green Fluorescent Protein 3D structures\|Green Fluorescent Protein 3D structures]]		*[[Green Fluorescent Protein 3D structures\|Green Fluorescent Protein 3D structures]]
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 15:09, 14 March 2024

2024-03-14T15:09:31Z

← Older revision		Revision as of 15:09, 14 March 2024
Line 10:		Line 10:
	== 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.
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Enhanced Green Fluorescent Protein (EGFP) is one of the most widely used engineered variants of the original wild-type Green Fluorescent Protein. Here, we report the high resolution (1.35 A) structure of EGFP crystallised in its untagged sequence form that reveals the combined impact of the F64L and S65T, that give rise to improved folding and spectral characteristics. The overall structure of EGFP is very similar to wt GFP, forming the classical beta-barrel fold with the chromophore containing helix running through the core of the structure. Replacement of Phe64 with Leu in EGFP results in subtle rearrangement of hydrophobic core packing close to the chromophore including the reduction in surface exposure of two hydrophobic residues. Replacement of Ser65 with Thr has a significant impact on the local hydrogen bond network in the vicinity of the chromophore. Detailed analysis of electron density reveals that several residues close to the chromophore occupy at least two distinct conformations. This includes Glu222 that defines the charged state on the chromophore, with the two conformations having slightly different effects on the hydrogen bond network surrounding the chromophore. Hence, the reported high-resolution structure of EGFP has provided a long overdue molecular description of one of the most important fluorescent protein variants currently in general use.

	Crystal structure of enhanced green fluorescent protein to 1.35 A resolution reveals alternative conformations for Glu222.,Arpino JA, Rizkallah PJ, Jones DD PLoS One. 2012;7(10):e47132. doi: 10.1371/journal.pone.0047132. Epub 2012 Oct 16. PMID:23077555<ref>PMID:23077555</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4eul" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Green Fluorescent Protein 3D structures\|Green Fluorescent Protein 3D structures]]		*[[Green Fluorescent Protein 3D structures\|Green Fluorescent Protein 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:21, 6 December 2023

2023-12-06T08:21:55Z

← Older revision		Revision as of 08:21, 6 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eul]] 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=4EUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EUL FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eul]] 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=4EUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EUL FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <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]] 1.35Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=4eul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eul OCA], [https://pdbe.org/4eul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eul RCSB], [https://www.ebi.ac.uk/pdbsum/4eul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eul 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=4eul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eul OCA], [https://pdbe.org/4eul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eul RCSB], [https://www.ebi.ac.uk/pdbsum/4eul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eul ProSAT]</span></td></tr>
	</table>		</table>

OCA at 04:17, 7 October 2022

2022-10-07T04:17:21Z

← Older revision		Revision as of 04:17, 7 October 2022
Line 1:		Line 1:

	==Crystal structure of enhanced Green Fluorescent Protein to 1.35A resolution reveals alternative conformations for Glu222==		==Crystal structure of enhanced Green Fluorescent Protein to 1.35A resolution reveals alternative conformations for Glu222==
	<StructureSection load='4eul' size='340' side='right' caption='[[4eul]], [[Resolution\|resolution]] 1.35Å' scene=''>		<StructureSection load='4eul' size='340' side='right'caption='[[4eul]], [[Resolution\|resolution]] 1.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eul]] is a 1 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=4EUL OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4EUL FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eul]] 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=4EUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EUL FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, ~~<scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4eul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eul OCA], [https://pdbe.org/4eul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eul RCSB], [https://www.ebi.ac.uk/pdbsum/4eul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eul ProSAT]</span></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='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=4eul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eul OCA], [~~http~~://pdbe.org/4eul PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4eul RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4eul PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4eul ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:

	==See Also==		==See Also==
	*[[Green Fluorescent Protein\|Green Fluorescent Protein]]		*[[Green Fluorescent Protein 3D structures\|Green Fluorescent Protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Aeqvi~~]]		[[Category: Aequorea victoria]]
	[[Category: ~~Arpino, J A.J~~]]		[[Category: Large Structures]]
	[[Category: ~~Jones, D D~~]]		[[Category: Arpino JAJ]]
	[[Category: ~~Rizkallah, P J~~]]		[[Category: Jones DD]]
	[[Category: ~~Beta barrel]]~~		[[Category: Rizkallah PJ]]
	~~[[Category: Cyclization of t65]]~~
	~~[[Category: Fluorescent protein]]~~
	~~[[Category: G67 backbone atom]]~~
	~~[[Category: Generating chromophore]]~~
	~~[[Category: Y66~~]]

OCA at 18:06, 4 August 2016

2016-08-04T18:06:49Z

← Older revision		Revision as of 18:06, 4 August 2016
Line 1:		Line 1:

	==Crystal structure of enhanced Green Fluorescent Protein to 1.35A resolution reveals alternative conformations for Glu222==		==Crystal structure of enhanced Green Fluorescent Protein to 1.35A resolution reveals alternative conformations for Glu222==
	<StructureSection load='4eul' size='340' side='right' caption='[[4eul]], [[Resolution\|resolution]] 1.35Å' scene=''>		<StructureSection load='4eul' size='340' side='right' caption='[[4eul]], [[Resolution\|resolution]] 1.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eul]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Aequorea_victoria Aequorea victoria~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EUL FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eul]] is a 1 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=4EUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EUL FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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>		<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>
	<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 ~~Aequorea victoria~~])</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='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=4eul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eul OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eul RCSB], [http://www.ebi.ac.uk/pdbsum/4eul PDBsum]</span></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=4eul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eul OCA], [http://pdbe.org/4eul PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4eul RCSB], [http://www.ebi.ac.uk/pdbsum/4eul PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4eul ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 4eul" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 25:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Aequorea victoria~~]]		[[Category: Aeqvi]]
	[[Category: Arpino, J A.J]]		[[Category: Arpino, J A.J]]
	[[Category: Jones, D D]]		[[Category: Jones, D D]]

OCA at 18:01, 24 December 2014

2014-12-24T18:01:00Z

← Older revision		Revision as of 18:01, 24 December 2014
Line 1:		Line 1:
	[[~~Image~~:~~4eul~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure of enhanced Green Fluorescent Protein to 1.35A resolution reveals alternative conformations for Glu222==
			<StructureSection load='4eul' size='340' side='right' caption='[[4eul]], [[Resolution\|resolution]] 1.35Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4eul]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EUL FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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>
			<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 Aequorea victoria])</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=4eul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eul OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eul RCSB], [http://www.ebi.ac.uk/pdbsum/4eul PDBsum]</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.
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Enhanced Green Fluorescent Protein (EGFP) is one of the most widely used engineered variants of the original wild-type Green Fluorescent Protein. Here, we report the high resolution (1.35 A) structure of EGFP crystallised in its untagged sequence form that reveals the combined impact of the F64L and S65T, that give rise to improved folding and spectral characteristics. The overall structure of EGFP is very similar to wt GFP, forming the classical beta-barrel fold with the chromophore containing helix running through the core of the structure. Replacement of Phe64 with Leu in EGFP results in subtle rearrangement of hydrophobic core packing close to the chromophore including the reduction in surface exposure of two hydrophobic residues. Replacement of Ser65 with Thr has a significant impact on the local hydrogen bond network in the vicinity of the chromophore. Detailed analysis of electron density reveals that several residues close to the chromophore occupy at least two distinct conformations. This includes Glu222 that defines the charged state on the chromophore, with the two conformations having slightly different effects on the hydrogen bond network surrounding the chromophore. Hence, the reported high-resolution structure of EGFP has provided a long overdue molecular description of one of the most important fluorescent protein variants currently in general use.

	~~{{STRUCTURE_4eul\| PDB=4eul \| SCENE= }}~~		Crystal structure of enhanced green fluorescent protein to 1.35 A resolution reveals alternative conformations for Glu222.,Arpino JA, Rizkallah PJ, Jones DD PLoS One. 2012;7(10):e47132. doi: 10.1371/journal.pone.0047132. Epub 2012 Oct 16. PMID:23077555<ref>PMID:23077555</ref>

	~~===Crystal structure~~ of ~~enhanced Green Fluorescent Protein to 1~~.~~35A resolution reveals alternative conformations for Glu222===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_23077555}}~~		==See Also==
			*[[Green Fluorescent Protein\|Green Fluorescent Protein]]
	==~~About this Structure~~==		== References ==
	[[~~4eul~~]] ~~is a 1 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EUL OCA].~~		<references/>
			__TOC__
			</StructureSection>
	[[Category: Aequorea victoria]]		[[Category: Aequorea victoria]]
	[[Category: Arpino, J A.J.]]		[[Category: Arpino, J A.J]]
	[[Category: Jones, D D.]]		[[Category: Jones, D D]]
	[[Category: Rizkallah, P J.]]		[[Category: Rizkallah, P J]]
	[[Category: Beta barrel]]		[[Category: Beta barrel]]
	[[Category: Cyclization of t65]]		[[Category: Cyclization of t65]]

OCA at 10:38, 19 December 2012

2012-12-19T10:38:14Z

← Older revision		Revision as of 10:38, 19 December 2012
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	[[Image:4eul.~~jpg~~\|left\|200px]]		[[Image:4eul.png\|left\|200px]]

	{{STRUCTURE_4eul\| PDB=4eul \| SCENE= }}		{{STRUCTURE_4eul\| PDB=4eul \| SCENE= }}
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	===Crystal structure of enhanced Green Fluorescent Protein to 1.35A resolution reveals alternative conformations for Glu222===		===Crystal structure of enhanced Green Fluorescent Protein to 1.35A resolution reveals alternative conformations for Glu222===

			{{ABSTRACT_PUBMED_23077555}}

	==About this Structure==		==About this Structure==

OCA at 06:25, 3 October 2012

2012-10-03T06:25:28Z

← Older revision		Revision as of 06:25, 3 October 2012
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	~~'''Unreleased structure'''~~		[[Image:4eul.jpg\|left\|200px]]

	~~The entry~~ 4eul ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4eul\| PDB=4eul \| SCENE= }}

	~~Authors: Jones, D.D., Arpino, J.A.J., Rizkallah, P.J~~.		===Crystal structure of enhanced Green Fluorescent Protein to 1.35A resolution reveals alternative conformations for Glu222===

	~~Description~~: ~~Crystal structure~~ of ~~enhanced Green~~ Fluorescent ~~Protein to 1.35A resolution reveals alternative conformations for Glu222~~
			==About this Structure==
			[[4eul]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EUL OCA].
			[[Category: Aequorea victoria]]
			[[Category: Arpino, J A.J.]]
			[[Category: Jones, D D.]]
			[[Category: Rizkallah, P J.]]
			[[Category: Beta barrel]]
			[[Category: Cyclization of t65]]
			[[Category: Fluorescent protein]]
			[[Category: G67 backbone atom]]
			[[Category: Generating chromophore]]
			[[Category: Y66]]

OCA at 07:45, 11 July 2012

2012-07-11T07:45:23Z

← Older revision		Revision as of 07:45, 11 July 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4eul is ON HOLD		The entry 4eul is ON HOLD until Paper Publication

	Authors: Jones, D.D., Arpino, J.A.J., Rizkallah, P.J.		Authors: Jones, D.D., Arpino, J.A.J., Rizkallah, P.J.

	Description: Crystal structure of enhanced Green Fluorescent Protein to 1.35A resolution reveals alternative conformations for Glu222		Description: Crystal structure of enhanced Green Fluorescent Protein to 1.35A resolution reveals alternative conformations for Glu222

OCA at 07:17, 6 June 2012

2012-06-06T07:17:36Z

← Older revision		Revision as of 07:17, 6 June 2012
Line 5:		Line 5:
	Authors: Jones, D.D., Arpino, J.A.J., Rizkallah, P.J.		Authors: Jones, D.D., Arpino, J.A.J., Rizkallah, P.J.

	Description: Crystal structure of enhanced Green Fluorescent Protein to 1.35 resolution reveals alternative conformations for Glu222		Description: Crystal structure of enhanced Green Fluorescent Protein to 1.35A resolution reveals alternative conformations for Glu222