1bx9 - Revision history

OCA at 15:36, 13 March 2024

OCA — Wed, 13 Mar 2024 15:36:53 GMT

←Older revision		Revision as of 15:36, 13 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1bx9]] is a 2 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=1BX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BX9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1bx9]] is a 2 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=1BX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BX9 FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non~~-~~Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOE:2-(2-AMINO-3-OXO-PROPYLSULFANYL)-N-(4-FLUORO-PHENYL)-N-ISOPROPYL-ACETAMIDE'>FOE</scene>, <scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</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]] 2.6Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FOE:2-(2-AMINO-3-OXO-PROPYLSULFANYL)-N-(4-FLUORO-PHENYL)-N-ISOPROPYL-ACETAMIDE'>FOE</scene>, <scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</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=1bx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bx9 OCA], [https://pdbe.org/1bx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bx9 RCSB], [https://www.ebi.ac.uk/pdbsum/1bx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bx9 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=1bx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bx9 OCA], [https://pdbe.org/1bx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bx9 RCSB], [https://www.ebi.ac.uk/pdbsum/1bx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bx9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/GSTF2_ARATH GSTF2_ARATH]] Binds auxin, endogenous flavonoids and the phytoalexin camalexin and may be involved in regulating the binding and transport of small bioactive natural products and defense-related compounds during plant stress. Binds a series of heterocyclic compounds, including lumichrome, harmane, norharmane and indole-3-aldehyde. In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). Acts as glutathione peroxidase on cumene hydroperoxide, linoleic acid-13-hydroperoxide and trans-stilbene oxide, but not trans-cinnamic acid or IAA-CoA.<ref>PMID:12090627</ref> <ref>PMID:21631432</ref>	+	[https://www.uniprot.org/uniprot/GSTF2_ARATH GSTF2_ARATH] Binds auxin, endogenous flavonoids and the phytoalexin camalexin and may be involved in regulating the binding and transport of small bioactive natural products and defense-related compounds during plant stress. Binds a series of heterocyclic compounds, including lumichrome, harmane, norharmane and indole-3-aldehyde. In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). Acts as glutathione peroxidase on cumene hydroperoxide, linoleic acid-13-hydroperoxide and trans-stilbene oxide, but not trans-cinnamic acid or IAA-CoA.<ref>PMID:12090627</ref> <ref>PMID:21631432</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bx9 ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bx9 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	BACKGROUND: Glutathione S-transferases (GSTs) are detoxifying enzymes present in all aerobic organisms. These enzymes catalyse the conjugation of glutathione with a variety of electrophilic compounds. In plants, GSTs catalyse the first step in the degradation of several herbicides, such as triazines and acetamides, thus playing an important role in herbicide tolerance. RESULTS: We have solved the structures of GST-I from maize in complex with an atrazine-glutathione conjugate (at 2.8 A resolution) and GST from Arabidopsis thaliana (araGST) in complex with an FOE-4053-glutathione conjugate (at 2.6 A resolution). These ligands are products of the detoxifying reaction and are well defined in the electron density. The herbicide-binding site (H site) is different in the two structures. The architecture of the glutathione-binding site (G site) of araGST is different to that of the previously described structure of GST in complex with two S-hexylglutathione molecules, but is homologous to that of GST-I. CONCLUSIONS: Three features are responsible for the differences in the H site of the two GSTs described here: the exchange of hydrophobic residues of different degrees of bulkiness; a slight difference in the location of the H site; and a difference in the degree of flexibility of the upper side of the H site, which is built up by the loop between helices alpha4 and alpha5. Taking these two structures as a model, the different substrate specificities of other plant GSTs may be explained. The structures reported here provide a basis for the design of new, more selective herbicides.
-
-	Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase - explanations for the selectivity of the enzyme in plants.,Prade L, Huber R, Bieseler B Structure. 1998 Nov 15;6(11):1445-52. PMID:9817846<ref>PMID:9817846</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1bx9" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 29:
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bieseler, B]]	+	[[Category: Bieseler B]]
-	[[Category: Huber, R]]	+	[[Category: Huber R]]
-	[[Category: Prade, L]]	+	[[Category: Prade L]]
-	~~[[Category: Foe-4053-glutathione conjugate]]~~	+
-	~~[[Category: Herbicide]]~~	+
-	~~[[Category: Product of the detoxifying reaction]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Transferase-peptide complex~~]]	+

OCA at 10:30, 14 July 2021

OCA — Wed, 14 Jul 2021 10:30:58 GMT

←Older revision		Revision as of 10:30, 14 July 2021
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	<StructureSection load='1bx9' size='340' side='right'caption='[[1bx9]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='1bx9' size='340' side='right'caption='[[1bx9]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1bx9]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1BX9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1bx9]] is a 2 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=1BX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BX9 FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOE:2-(2-AMINO-3-OXO-PROPYLSULFANYL)-N-(4-FLUORO-PHENYL)-N-ISOPROPYL-ACETAMIDE'>FOE</scene>, <scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOE:2-(2-AMINO-3-OXO-PROPYLSULFANYL)-N-(4-FLUORO-PHENYL)-N-ISOPROPYL-ACETAMIDE'>FOE</scene>, <scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</scene></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=1bx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bx9 OCA], [~~http~~://pdbe.org/1bx9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1bx9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1bx9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1bx9 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=1bx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bx9 OCA], [https://pdbe.org/1bx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bx9 RCSB], [https://www.ebi.ac.uk/pdbsum/1bx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bx9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/GSTF2_ARATH GSTF2_ARATH]] Binds auxin, endogenous flavonoids and the phytoalexin camalexin and may be involved in regulating the binding and transport of small bioactive natural products and defense-related compounds during plant stress. Binds a series of heterocyclic compounds, including lumichrome, harmane, norharmane and indole-3-aldehyde. In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). Acts as glutathione peroxidase on cumene hydroperoxide, linoleic acid-13-hydroperoxide and trans-stilbene oxide, but not trans-cinnamic acid or IAA-CoA.<ref>PMID:12090627</ref> <ref>PMID:21631432</ref>	+	[[https://www.uniprot.org/uniprot/GSTF2_ARATH GSTF2_ARATH]] Binds auxin, endogenous flavonoids and the phytoalexin camalexin and may be involved in regulating the binding and transport of small bioactive natural products and defense-related compounds during plant stress. Binds a series of heterocyclic compounds, including lumichrome, harmane, norharmane and indole-3-aldehyde. In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). Acts as glutathione peroxidase on cumene hydroperoxide, linoleic acid-13-hydroperoxide and trans-stilbene oxide, but not trans-cinnamic acid or IAA-CoA.<ref>PMID:12090627</ref> <ref>PMID:21631432</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:28, 10 October 2019

OCA — Thu, 10 Oct 2019 07:28:52 GMT

←Older revision		Revision as of 07:28, 10 October 2019
Line 1:		Line 1:

	==GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH HERBICIDE==		==GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH HERBICIDE==
-	<StructureSection load='1bx9' size='340' side='right' caption='[[1bx9]], [[Resolution\|resolution]] 2.60Å' scene=''>	+	<StructureSection load='1bx9' size='340' side='right'caption='[[1bx9]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1bx9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BX9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1bx9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BX9 FirstGlance]. <br>
Line 13:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bx/1bx9_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bx/1bx9_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 28:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1bx9" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1bx9" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glutathione S-transferase 3D structures\|Glutathione S-transferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
		+	[[Category: Large Structures]]
	[[Category: Bieseler, B]]		[[Category: Bieseler, B]]
	[[Category: Huber, R]]		[[Category: Huber, R]]

OCA at 08:19, 29 November 2017

OCA — Wed, 29 Nov 2017 08:19:12 GMT

←Older revision		Revision as of 08:19, 29 November 2017
Line 1:		Line 1:
		+
	==GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH HERBICIDE==		==GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH HERBICIDE==
	<StructureSection load='1bx9' size='340' side='right' caption='[[1bx9]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='1bx9' size='340' side='right' caption='[[1bx9]], [[Resolution\|resolution]] 2.60Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1bx9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BX9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1bx9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BX9 FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOE:2-(2-AMINO-3-OXO-PROPYLSULFANYL)-N-(4-FLUORO-PHENYL)-N-ISOPROPYL-ACETAMIDE'>FOE</scene>, <scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOE:2-(2-AMINO-3-OXO-PROPYLSULFANYL)-N-(4-FLUORO-PHENYL)-N-ISOPROPYL-ACETAMIDE'>FOE</scene>, <scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</scene></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=1bx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bx9 OCA], [http://pdbe.org/1bx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bx9 RCSB], [http://www.ebi.ac.uk/pdbsum/1bx9 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=1bx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bx9 OCA], [http://pdbe.org/1bx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bx9 RCSB], [http://www.ebi.ac.uk/pdbsum/1bx9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bx9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1bx9" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1bx9" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Glutathione S-transferase\|Glutathione S-transferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 05:35, 10 February 2016

OCA — Wed, 10 Feb 2016 05:35:34 GMT

←Older revision		Revision as of 05:35, 10 February 2016
Line 16:		Line 16:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bx9 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 05:52, 11 September 2015

OCA — Fri, 11 Sep 2015 05:52:40 GMT

←Older revision		Revision as of 05:52, 11 September 2015
Line 4:		Line 4:
	<table><tr><td colspan='2'>[[1bx9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BX9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1bx9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BX9 FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOE:2-(2-AMINO-3-OXO-PROPYLSULFANYL)-N-(4-FLUORO-PHENYL)-N-ISOPROPYL-ACETAMIDE'>FOE</scene>, <scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOE:2-(2-AMINO-3-OXO-PROPYLSULFANYL)-N-(4-FLUORO-PHENYL)-N-ISOPROPYL-ACETAMIDE'>FOE</scene>, <scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</scene></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=1bx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bx9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bx9 RCSB], [http://www.ebi.ac.uk/pdbsum/1bx9 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=1bx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bx9 OCA], [http://pdbe.org/1bx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bx9 RCSB], [http://www.ebi.ac.uk/pdbsum/1bx9 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GSTF2_ARATH GSTF2_ARATH]] Binds auxin, endogenous flavonoids and the phytoalexin camalexin and may be involved in regulating the binding and transport of small bioactive natural products and defense-related compounds during plant stress. Binds a series of heterocyclic compounds, including lumichrome, harmane, norharmane and indole-3-aldehyde. In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). Acts as glutathione peroxidase on cumene hydroperoxide, linoleic acid-13-hydroperoxide and trans-stilbene oxide, but not trans-cinnamic acid or IAA-CoA.<ref>PMID:12090627</ref> <ref>PMID:21631432</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 24:		Line 26:
	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 1bx9" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 10:24, 22 December 2014

OCA — Mon, 22 Dec 2014 10:24:12 GMT

←Older revision		Revision as of 10:24, 22 December 2014
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1bx9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BX9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1bx9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BX9 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOE:2-(2-AMINO-3-OXO-PROPYLSULFANYL)-N-(4-FLUORO-PHENYL)-N-ISOPROPYL-ACETAMIDE'>FOE</scene>, <scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOE:2-(2-AMINO-3-OXO-PROPYLSULFANYL)-N-(4-FLUORO-PHENYL)-N-ISOPROPYL-ACETAMIDE'>FOE</scene>, <scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bx9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bx9 RCSB], [http://www.ebi.ac.uk/pdbsum/1bx9 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=1bx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bx9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bx9 RCSB], [http://www.ebi.ac.uk/pdbsum/1bx9 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
-	[[Category: Bieseler, B.]]	+	[[Category: Bieseler, B]]
-	[[Category: Huber, R.]]	+	[[Category: Huber, R]]
-	[[Category: Prade, L.]]	+	[[Category: Prade, L]]
	[[Category: Foe-4053-glutathione conjugate]]		[[Category: Foe-4053-glutathione conjugate]]
	[[Category: Herbicide]]		[[Category: Herbicide]]

OCA at 09:47, 13 August 2014

OCA — Wed, 13 Aug 2014 09:47:58 GMT

←Older revision		Revision as of 09:47, 13 August 2014
Line 1:		Line 1:
-	[[~~Image~~:1bx9.~~png\|left~~\|200px]]	+	==GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH HERBICIDE==
		+	<StructureSection load='1bx9' size='340' side='right' caption='[[1bx9]], [[Resolution\|resolution]] 2.60Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1bx9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BX9 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOE:2-(2-AMINO-3-OXO-PROPYLSULFANYL)-N-(4-FLUORO-PHENYL)-N-ISOPROPYL-ACETAMIDE'>FOE</scene>, <scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bx9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bx9 RCSB], [http://www.ebi.ac.uk/pdbsum/1bx9 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bx/1bx9_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	BACKGROUND: Glutathione S-transferases (GSTs) are detoxifying enzymes present in all aerobic organisms. These enzymes catalyse the conjugation of glutathione with a variety of electrophilic compounds. In plants, GSTs catalyse the first step in the degradation of several herbicides, such as triazines and acetamides, thus playing an important role in herbicide tolerance. RESULTS: We have solved the structures of GST-I from maize in complex with an atrazine-glutathione conjugate (at 2.8 A resolution) and GST from Arabidopsis thaliana (araGST) in complex with an FOE-4053-glutathione conjugate (at 2.6 A resolution). These ligands are products of the detoxifying reaction and are well defined in the electron density. The herbicide-binding site (H site) is different in the two structures. The architecture of the glutathione-binding site (G site) of araGST is different to that of the previously described structure of GST in complex with two S-hexylglutathione molecules, but is homologous to that of GST-I. CONCLUSIONS: Three features are responsible for the differences in the H site of the two GSTs described here: the exchange of hydrophobic residues of different degrees of bulkiness; a slight difference in the location of the H site; and a difference in the degree of flexibility of the upper side of the H site, which is built up by the loop between helices alpha4 and alpha5. Taking these two structures as a model, the different substrate specificities of other plant GSTs may be explained. The structures reported here provide a basis for the design of new, more selective herbicides.

-	~~{{STRUCTURE_1bx9\| PDB=1bx9 \| SCENE= }}~~	+	Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase - explanations for the selectivity of the enzyme in plants.,Prade L, Huber R, Bieseler B Structure. 1998 Nov 15;6(11):1445-52. PMID:9817846<ref>PMID:9817846</ref>

-	~~===GLUTATHIONE~~ S~~-TRANSFERASE IN COMPLEX WITH HERBICIDE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_9817846}}~~	+	==See Also==
-		+	*[[Glutathione S-transferase\|Glutathione S-transferase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1bx9~~]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX9 OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:009817846<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
	[[Category: Bieseler, B.]]		[[Category: Bieseler, B.]]

OCA: Protected "1bx9" [edit=sysop:move=sysop]

OCA — Sun, 21 Oct 2012 20:53:34 GMT

Protected "1bx9" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:53, 21 October 2012

OCA at 20:53, 21 October 2012

OCA — Sun, 21 Oct 2012 20:53:32 GMT

←Older revision		Revision as of 20:53, 21 October 2012
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-	{{Seed}}
	[[Image:1bx9.png\|left\|200px]]		[[Image:1bx9.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1bx9", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1bx9\| PDB=1bx9 \| SCENE= }}		{{STRUCTURE_1bx9\| PDB=1bx9 \| SCENE= }}

	===GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH HERBICIDE===		===GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH HERBICIDE===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_9817846}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 9817846 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_9817846}}		{{ABSTRACT_PUBMED_9817846}}

	==About this Structure==		==About this Structure==
-	~~1BX9~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX9 OCA].	+	[[1bx9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX9 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~9817846~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:009817846</ref><references group="xtra"/>
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
	[[Category: Bieseler, B.]]		[[Category: Bieseler, B.]]
	[[Category: Huber, R.]]		[[Category: Huber, R.]]
	[[Category: Prade, L.]]		[[Category: Prade, L.]]
-	[[Category: ~~Glutathione~~]]	+	[[Category: Foe-4053-glutathione conjugate]]
	[[Category: Herbicide]]		[[Category: Herbicide]]
		+	[[Category: Product of the detoxifying reaction]]
	[[Category: Transferase]]		[[Category: Transferase]]
-		+	[[Category: Transferase-peptide complex]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 15:49:42 2009''~~	+