8aib - Revision history

OCA at 08:12, 7 February 2024

2024-02-07T08:12:04Z

← Older revision		Revision as of 08:12, 7 February 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8aib]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AIB FirstGlance]. <br>		<table><tr><td colspan='2'>[[8aib]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AIB FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</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]] 2.2Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</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=8aib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aib OCA], [https://pdbe.org/8aib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aib RCSB], [https://www.ebi.ac.uk/pdbsum/8aib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aib 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=8aib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aib OCA], [https://pdbe.org/8aib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aib RCSB], [https://www.ebi.ac.uk/pdbsum/8aib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aib ProSAT]</span></td></tr>
	</table>		</table>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Glutathione transferases (GSTs) constitute a widespread superfamily of enzymes notably involved in detoxification processes and/or in specialized metabolism. In the cyanobacterium Synechocsytis sp. PCC 6803, SynGSTC1, a chi-class GST (GSTC), is thought to participate in the detoxification process of methylglyoxal, a toxic by-product of cellular metabolism. A comparative genomic analysis showed that GSTCs were present in all orders of cyanobacteria with the exception of the basal order Gloeobacterales. These enzymes were also detected in some marine and freshwater noncyanobacterial bacteria, probably as a result of horizontal gene transfer events. GSTCs were shorter of about 30 residues compared to most cytosolic GSTs and had a well-conserved SRAS motif in the active site ((10)SRAS(13) in SynGSTC1). The crystal structure of SynGSTC1 in complex with glutathione adopted the canonical GST fold with a very open active site because the alpha4 and alpha5 helices were exceptionally short. A transferred multipolar electron-density analysis allowed a fine description of the solved structure. Unexpectedly, Ser10 did not have an electrostatic influence on glutathione as usually observed in serinyl-GSTs. The S10A variant was only slightly less efficient than the wild-type and molecular dynamics simulations suggested that S10 was a stabilizer of the protein backbone rather than an anchor site for glutathione.

	Biochemical and Structural Characterization of Chi-Class Glutathione Transferases: A Snapshot on the Glutathione Transferase Encoded by sll0067 Gene in the Cyanobacterium Synechocystis sp. Strain PCC 6803.,Mocchetti E, Morette L, Mulliert G, Mathiot S, Guillot B, Dehez F, Chauvat F, Cassier-Chauvat C, Brochier-Armanet C, Didierjean C, Hecker A Biomolecules. 2022 Oct 13;12(10):1466. doi: 10.3390/biom12101466. PMID:36291676<ref>PMID:36291676</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 8aib" style="background-color:#fffaf0;"></div>~~
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 05:37, 31 May 2023

2023-05-31T05:37:48Z

← Older revision		Revision as of 05:37, 31 May 2023
Line 1:		Line 1:
	~~'''Unreleased structure'''~~

	~~The entry~~ 8aib is ~~ON HOLD until Paper~~ Publication		==R11A variant of glutathione transferase Chi 1 from Synechocystis sp. PCC 6803 in complex with glutathione==
			<StructureSection load='8aib' size='340' side='right'caption='[[8aib]], [[Resolution\|resolution]] 2.20Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[8aib]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AIB FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</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=8aib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aib OCA], [https://pdbe.org/8aib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aib RCSB], [https://www.ebi.ac.uk/pdbsum/8aib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aib ProSAT]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Glutathione transferases (GSTs) constitute a widespread superfamily of enzymes notably involved in detoxification processes and/or in specialized metabolism. In the cyanobacterium Synechocsytis sp. PCC 6803, SynGSTC1, a chi-class GST (GSTC), is thought to participate in the detoxification process of methylglyoxal, a toxic by-product of cellular metabolism. A comparative genomic analysis showed that GSTCs were present in all orders of cyanobacteria with the exception of the basal order Gloeobacterales. These enzymes were also detected in some marine and freshwater noncyanobacterial bacteria, probably as a result of horizontal gene transfer events. GSTCs were shorter of about 30 residues compared to most cytosolic GSTs and had a well-conserved SRAS motif in the active site ((10)SRAS(13) in SynGSTC1). The crystal structure of SynGSTC1 in complex with glutathione adopted the canonical GST fold with a very open active site because the alpha4 and alpha5 helices were exceptionally short. A transferred multipolar electron-density analysis allowed a fine description of the solved structure. Unexpectedly, Ser10 did not have an electrostatic influence on glutathione as usually observed in serinyl-GSTs. The S10A variant was only slightly less efficient than the wild-type and molecular dynamics simulations suggested that S10 was a stabilizer of the protein backbone rather than an anchor site for glutathione.

	~~Authors~~: ~~Diddierjean~~, C.		Biochemical and Structural Characterization of Chi-Class Glutathione Transferases: A Snapshot on the Glutathione Transferase Encoded by sll0067 Gene in the Cyanobacterium Synechocystis sp. Strain PCC 6803.,Mocchetti E, Morette L, Mulliert G, Mathiot S, Guillot B, Dehez F, Chauvat F, Cassier-Chauvat C, Brochier-Armanet C, Didierjean C, Hecker A Biomolecules. 2022 Oct 13;12(10):1466. doi: 10.3390/biom12101466. PMID:36291676<ref>PMID:36291676</ref>

	~~Description: R11A variant~~ of ~~glutathione transferase Chi 1 from Synechocystis sp~~. ~~PCC 6803 in complex with glutathione~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	[[Category: ~~Unreleased~~ Structures]]		</div>
	[[Category: ~~Diddierjean,~~ C]]		<div class="pdbe-citations 8aib" style="background-color:#fffaf0;"></div>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
			[[Category: Large Structures]]
			[[Category: Synechocystis sp. PCC 6803]]
			[[Category: Didierjean C]]

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

2022-08-03T03:48:34Z

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

← Older revision	Revision as of 03:48, 3 August 2022
(No difference)

OCA: New page: '''Unreleased structure''' The entry 8aib is ON HOLD until Paper Publication Authors: Diddierjean, C. Description: R11A variant of glutathione transferase Chi 1 from Synechocystis sp. ...

2022-08-03T03:48:33Z

New page: '''Unreleased structure''' The entry 8aib is ON HOLD until Paper Publication Authors: Diddierjean, C. Description: R11A variant of glutathione transferase Chi 1 from Synechocystis sp. ...

New page

'''Unreleased structure'''

The entry 8aib is ON HOLD until Paper Publication

Authors: Diddierjean, C.

Description: R11A variant of glutathione transferase Chi 1 from Synechocystis sp. PCC 6803 in complex with glutathione
[[Category: Unreleased Structures]]
[[Category: Diddierjean, C]]