8a4e - Revision history

OCA at 08:08, 7 February 2024

2024-02-07T08:08:44Z

←Older revision		Revision as of 08:08, 7 February 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8a4e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A4E FirstGlance]. <br>		<table><tr><td colspan='2'>[[8a4e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A4E FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMA:6-(3-TETRADECANOIC+ACID)+FLAVINE+MONONUCLEOTIDE'>FMA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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]] 1.96Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMA:6-(3-TETRADECANOIC+ACID)+FLAVINE+MONONUCLEOTIDE'>FMA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=8a4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a4e OCA], [https://pdbe.org/8a4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a4e RCSB], [https://www.ebi.ac.uk/pdbsum/8a4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a4e 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=8a4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a4e OCA], [https://pdbe.org/8a4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a4e RCSB], [https://www.ebi.ac.uk/pdbsum/8a4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a4e ProSAT]</span></td></tr>
	</table>		</table>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The development of serial crystallography over the last decade at XFELs and synchrotrons has produced a renaissance in room-temperature macromolecular crystallography (RT-MX), and fostered many technical and methodological breakthroughs designed to study phenomena occurring in proteins on the picosecond-to-second timescale. However, there are components of protein dynamics that occur in much slower regimes, of which the study could readily benefit from state-of-the-art RT-MX. Here, the room-temperature structural study of the relaxation of a reaction intermediate at a synchrotron, exploiting a handful of single crystals, is described. The intermediate in question is formed in microseconds during the photoreaction of the LOV2 domain of phototropin 2 from Arabidopsis thaliana, which then decays in minutes. This work monitored its relaxation in the dark using a fast-readout EIGER X 4M detector to record several complete oscillation X-ray diffraction datasets, each of 1.2 s total exposure time, at different time points in the relaxation process. Coupled with in crystallo UV-Vis absorption spectroscopy, this RT-MX approach allowed the authors to follow the relaxation of the photoadduct, a thio-ether covalent bond between the chromophore and a cysteine residue. Unexpectedly, the return of the chromophore to its spectroscopic ground state is followed by medium-scale protein rearrangements that trigger a crystal phase transition and hinder the full recovery of the structural ground state of the protein. In addition to suggesting a hitherto unexpected role of a conserved tryptophan residue in the regulation of the photocycle of LOV2, this work provides a basis for performing routine time-resolved protein crystallography experiments at synchrotrons for phenomena occurring on the second-to-hour timescale.
-
-	Slow protein dynamics probed by time-resolved oscillation crystallography at room temperature.,Aumonier S, Engilberge S, Caramello N, von Stetten D, Gotthard G, Leonard GA, Mueller-Dieckmann C, Royant A IUCrJ. 2022 Sep 28;9(Pt 6):756-767. doi: 10.1107/S2052252522009150. eCollection , 2022 Nov 1. PMID:36381146<ref>PMID:36381146</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 8a4e" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:46, 29 March 2023

2023-03-29T06:46:39Z

←Older revision		Revision as of 06:46, 29 March 2023
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-	'''Unreleased structure'''

-	~~The entry~~ 8a4e is ~~ON HOLD until Paper~~ Publication	+	==Room temperature structure of AtPhot2LOV2 in a photostationary equilibrium==
		+	<StructureSection load='8a4e' size='340' side='right'caption='[[8a4e]], [[Resolution\|resolution]] 1.96Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8a4e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A4E FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMA:6-(3-TETRADECANOIC+ACID)+FLAVINE+MONONUCLEOTIDE'>FMA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=8a4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a4e OCA], [https://pdbe.org/8a4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a4e RCSB], [https://www.ebi.ac.uk/pdbsum/8a4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a4e ProSAT]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The development of serial crystallography over the last decade at XFELs and synchrotrons has produced a renaissance in room-temperature macromolecular crystallography (RT-MX), and fostered many technical and methodological breakthroughs designed to study phenomena occurring in proteins on the picosecond-to-second timescale. However, there are components of protein dynamics that occur in much slower regimes, of which the study could readily benefit from state-of-the-art RT-MX. Here, the room-temperature structural study of the relaxation of a reaction intermediate at a synchrotron, exploiting a handful of single crystals, is described. The intermediate in question is formed in microseconds during the photoreaction of the LOV2 domain of phototropin 2 from Arabidopsis thaliana, which then decays in minutes. This work monitored its relaxation in the dark using a fast-readout EIGER X 4M detector to record several complete oscillation X-ray diffraction datasets, each of 1.2 s total exposure time, at different time points in the relaxation process. Coupled with in crystallo UV-Vis absorption spectroscopy, this RT-MX approach allowed the authors to follow the relaxation of the photoadduct, a thio-ether covalent bond between the chromophore and a cysteine residue. Unexpectedly, the return of the chromophore to its spectroscopic ground state is followed by medium-scale protein rearrangements that trigger a crystal phase transition and hinder the full recovery of the structural ground state of the protein. In addition to suggesting a hitherto unexpected role of a conserved tryptophan residue in the regulation of the photocycle of LOV2, this work provides a basis for performing routine time-resolved protein crystallography experiments at synchrotrons for phenomena occurring on the second-to-hour timescale.

-	~~Authors: Engilberge~~, S., ~~Caramello~~, N., ~~Royant~~, A.	+	Slow protein dynamics probed by time-resolved oscillation crystallography at room temperature.,Aumonier S, Engilberge S, Caramello N, von Stetten D, Gotthard G, Leonard GA, Mueller-Dieckmann C, Royant A IUCrJ. 2022 Sep 28;9(Pt 6):756-767. doi: 10.1107/S2052252522009150. eCollection , 2022 Nov 1. PMID:36381146<ref>PMID:36381146</ref>

-	~~Description: Room temperature structure of AtPhot2LOV2 in~~ a ~~photostationary equilibrium~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
-	[[Category: Caramello, N]]	+	<div class="pdbe-citations 8a4e" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Royant, A~~]]	+	== References ==
-	[[Category: ~~Engilberge, S~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Arabidopsis thaliana]]
		+	[[Category: Large Structures]]
		+	[[Category: Caramello N]]
		+	[[Category: Engilberge S]]
		+	[[Category: Royant A]]

OCA at 04:10, 20 July 2022

2022-07-20T04:10:59Z

←Older revision		Revision as of 04:10, 20 July 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8a4e is ON HOLD	+	The entry 8a4e is ON HOLD until Paper Publication

	Authors: Engilberge, S., Caramello, N., Royant, A.		Authors: Engilberge, S., Caramello, N., Royant, A.

OCA: Protected "8a4e" [edit=sysop:move=sysop]

2022-06-22T07:18:37Z

Protected "8a4e" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:18, 22 June 2022

OCA: New page: '''Unreleased structure''' The entry 8a4e is ON HOLD Authors: Engilberge, S., Caramello, N., Royant, A. Description: Room temperature structure of AtPhot2LOV2 in a photostationary equi...

2022-06-22T07:18:36Z

New page: '''Unreleased structure''' The entry 8a4e is ON HOLD Authors: Engilberge, S., Caramello, N., Royant, A. Description: Room temperature structure of AtPhot2LOV2 in a photostationary equi...

New page

'''Unreleased structure'''

The entry 8a4e is ON HOLD

Authors: Engilberge, S., Caramello, N., Royant, A.

Description: Room temperature structure of AtPhot2LOV2 in a photostationary equilibrium
[[Category: Unreleased Structures]]
[[Category: Caramello, N]]
[[Category: Royant, A]]
[[Category: Engilberge, S]]