8bhc - Revision history

OCA at 08:18, 7 February 2024

2024-02-07T08:18:22Z

←Older revision		Revision as of 08:18, 7 February 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8bhc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BHC FirstGlance]. <br>		<table><tr><td colspan='2'>[[8bhc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BHC FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</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]] 1.56Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</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=8bhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bhc OCA], [https://pdbe.org/8bhc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bhc RCSB], [https://www.ebi.ac.uk/pdbsum/8bhc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bhc 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=8bhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bhc OCA], [https://pdbe.org/8bhc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bhc RCSB], [https://www.ebi.ac.uk/pdbsum/8bhc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bhc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/GSTA1_HUMAN GSTA1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:20606271</ref>		[https://www.uniprot.org/uniprot/GSTA1_HUMAN GSTA1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:20606271</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Glutathione transferases (GSTs) are promiscuous enzymes whose main function is the detoxification of electrophilic compounds. These enzymes are characterized by structural modularity that underpins their exploitation as dynamic scaffolds for engineering enzyme variants, with customized catalytic and structural properties. In the present work, multiple sequence alignment of the alpha class GSTs allowed the identification of three conserved residues (E137, K141, and S142) at alpha-helix 5 (H5). A motif-directed redesign of the human glutathione transferase A1-1 (hGSTA1-1) was performed through site-directed mutagenesis at these sites, creating two single- and two double-point mutants (E137H, K141H, K141H/S142H, and E137H/K141H). The results showed that all the enzyme variants displayed enhanced catalytic activity compared to the wild-type enzyme hGSTA1-1, while the double mutant hGSTA1-K141H/S142H also showed improved thermal stability. X-ray crystallographic analysis revealed the molecular basis of the effects of double mutations on enzyme stability and catalysis. The biochemical and structural analysis presented here will contribute to a deeper understanding of the structure and function of alpha class GSTs.

-	A Key Role in Catalysis and Enzyme Thermostability of a Conserved Helix H5 Motif of Human Glutathione Transferase A1-1.,Chronopoulou EG, Mutabdzija L, Poudel N, Papageorgiou AC, Labrou NE Int J Mol Sci. 2023 Feb 12;24(4):3700. doi: 10.3390/ijms24043700. PMID:36835112<ref>PMID:36835112</ref>	+	==See Also==
-		+	*[[Glutathione S-transferase 3D structures\|Glutathione S-transferase 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.~~S~~. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe~~-~~citations 8bhc" style="background~~-~~color:#fffaf0;"></div>~~	+
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:32, 8 March 2023

2023-03-08T07:32:04Z

←Older revision		Revision as of 07:32, 8 March 2023
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 8bhc is ~~ON HOLD until Paper~~ Publication	+	==K141H and S142H double mutant of hGSTA1-1==
		+	<StructureSection load='8bhc' size='340' side='right'caption='[[8bhc]], [[Resolution\|resolution]] 1.56Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8bhc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BHC FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</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=8bhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bhc OCA], [https://pdbe.org/8bhc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bhc RCSB], [https://www.ebi.ac.uk/pdbsum/8bhc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bhc ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/GSTA1_HUMAN GSTA1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:20606271</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Glutathione transferases (GSTs) are promiscuous enzymes whose main function is the detoxification of electrophilic compounds. These enzymes are characterized by structural modularity that underpins their exploitation as dynamic scaffolds for engineering enzyme variants, with customized catalytic and structural properties. In the present work, multiple sequence alignment of the alpha class GSTs allowed the identification of three conserved residues (E137, K141, and S142) at alpha-helix 5 (H5). A motif-directed redesign of the human glutathione transferase A1-1 (hGSTA1-1) was performed through site-directed mutagenesis at these sites, creating two single- and two double-point mutants (E137H, K141H, K141H/S142H, and E137H/K141H). The results showed that all the enzyme variants displayed enhanced catalytic activity compared to the wild-type enzyme hGSTA1-1, while the double mutant hGSTA1-K141H/S142H also showed improved thermal stability. X-ray crystallographic analysis revealed the molecular basis of the effects of double mutations on enzyme stability and catalysis. The biochemical and structural analysis presented here will contribute to a deeper understanding of the structure and function of alpha class GSTs.

-	~~Authors: Papageorgiou,~~ A.C., ~~Poudel~~, N.	+	A Key Role in Catalysis and Enzyme Thermostability of a Conserved Helix H5 Motif of Human Glutathione Transferase A1-1.,Chronopoulou EG, Mutabdzija L, Poudel N, Papageorgiou AC, Labrou NE Int J Mol Sci. 2023 Feb 12;24(4):3700. doi: 10.3390/ijms24043700. PMID:36835112<ref>PMID:36835112</ref>

-	~~Description: K141H and S142H double mutant~~ of ~~hGSTA1~~-1	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
-	[[Category: Papageorgiou~~, A.C~~]]	+	<div class="pdbe-citations 8bhc" style="background-color:#fffaf0;"></div>
-	[[Category: Poudel, N]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
		+	[[Category: Papageorgiou AC]]
		+	[[Category: Poudel N]]

OCA at 05:09, 7 December 2022

2022-12-07T05:09:11Z

←Older revision		Revision as of 05:09, 7 December 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Papageorgiou, A.C., Poudel, N.		Authors: Papageorgiou, A.C., Poudel, N.

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

2022-11-09T04:53:59Z

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

←Older revision

Revision as of 04:53, 9 November 2022

OCA: New page: '''Unreleased structure''' The entry 8bhc is ON HOLD Authors: Papageorgiou, A.C., Poudel, N. Description: K141H and S142H double mutant of hGSTA1-1 Category: Unreleased Structures ...

2022-11-09T04:53:58Z

New page: '''Unreleased structure''' The entry 8bhc is ON HOLD Authors: Papageorgiou, A.C., Poudel, N. Description: K141H and S142H double mutant of hGSTA1-1 Category: Unreleased Structures ...

New page

'''Unreleased structure'''

The entry 8bhc is ON HOLD

Authors: Papageorgiou, A.C., Poudel, N.

Description: K141H and S142H double mutant of hGSTA1-1
[[Category: Unreleased Structures]]
[[Category: Papageorgiou, A.C]]
[[Category: Poudel, N]]