5f8b - Revision history

OCA at 09:11, 20 March 2024

OCA — Wed, 20 Mar 2024 09:11:47 GMT

←Older revision		Revision as of 09:11, 20 March 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/PSOE_ASPFU PSOE_ASPFU] Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation (PubMed:24082142, PubMed:24939566). The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566). The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566). Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566, PubMed:27072782). The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566). Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566).<ref>PMID:24082142</ref> <ref>PMID:24939566</ref> <ref>PMID:27072782</ref>		[https://www.uniprot.org/uniprot/PSOE_ASPFU PSOE_ASPFU] Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation (PubMed:24082142, PubMed:24939566). The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566). The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566). Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566, PubMed:27072782). The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566). Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566).<ref>PMID:24082142</ref> <ref>PMID:24939566</ref> <ref>PMID:27072782</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Geometric isomerization can expand the scope of biological activities of natural products. The observed chemical diversity among the pseurotin-type fungal secondary metabolites is in part generated by a trans to cis isomerization of an olefin. In vitro characterizations of pseurotin biosynthetic enzymes revealed that the glutathione S-transferase PsoE requires participation of the bifunctional C-methyltransferase/epoxidase PsoF to complete the trans to cis isomerization of the pathway intermediate presynerazol. The crystal structure of the PsoE/glutathione/presynerazol complex indicated stereospecific glutathione-presynerazol conjugate formation is the principal function of PsoE. Moreover, PsoF was identified to have an additional, unexpected oxidative isomerase activity, thus making it a trifunctional enzyme which is key to the complexity generation in pseurotin biosynthesis. Through the study, we identified a novel mechanism of accomplishing a seemingly simple trans to cis isomerization reaction.
-
-	Oxidative trans to cis Isomerization of Olefins in Polyketide Biosynthesis.,Yamamoto T, Tsunematsu Y, Hara K, Suzuki T, Kishimoto S, Kawagishi H, Noguchi H, Hashimoto H, Tang Y, Hotta K, Watanabe K Angew Chem Int Ed Engl. 2016 May 17;55(21):6207-10. doi: 10.1002/anie.201600940. , Epub 2016 Apr 13. PMID:27072782<ref>PMID:27072782</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5f8b" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:41, 19 July 2023

OCA — Wed, 19 Jul 2023 06:41:53 GMT

←Older revision		Revision as of 06:41, 19 July 2023
Line 1:		Line 1:

	==Crystallographic Structure of PsoE with Co==		==Crystallographic Structure of PsoE with Co==
-	<StructureSection load='5f8b' size='340' side='right' caption='[[5f8b]], [[Resolution\|resolution]] 2.54Å' scene=''>	+	<StructureSection load='5f8b' size='340' side='right'caption='[[5f8b]], [[Resolution\|resolution]] 2.54Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5f8b]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Aspfu Aspfu~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8B OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5F8B FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5f8b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus_Af293 Aspergillus fumigatus Af293]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F8B FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=PZS:(5~{S},8~{S},9~{R})-2-[(~{E})-HEX-1-ENYL]-8-METHOXY-3-METHYL-9-OXIDANYL-8-(PHENYLCARBONYL)-1-OXA-7-AZASPIRO[4.4]NON-2-ENE-4,6-DIONE'>PZS</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]] 2.54Å</td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AFUA_8G00580 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=330879 ASPFU])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=PZS:(5~{S},8~{S},9~{R})-2-[(~{E})-HEX-1-ENYL]-8-METHOXY-3-METHYL-9-OXIDANYL-8-(PHENYLCARBONYL)-1-OXA-7-AZASPIRO[4.4]NON-2-ENE-4,6-DIONE'>PZS</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=5f8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8b OCA], [~~http~~://pdbe.org/5f8b PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5f8b RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5f8b PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8b 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=5f8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8b OCA], [https://pdbe.org/5f8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f8b RCSB], [https://www.ebi.ac.uk/pdbsum/5f8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8b ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/PSOE_ASPFU PSOE_ASPFU] Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation (PubMed:24082142, PubMed:24939566). The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566). The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566). Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566, PubMed:27072782). The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566). Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566).<ref>PMID:24082142</ref> <ref>PMID:24939566</ref> <ref>PMID:27072782</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Aspfu~~]]	+	[[Category: Aspergillus fumigatus Af293]]
-	[[Category: Hara, K]]	+	[[Category: Large Structures]]
-	[[Category: Hashimoto, H]]	+	[[Category: Hara K]]
-	[[Category: Tsunematsu, Y]]	+	[[Category: Hashimoto H]]
-	[[Category: Watanabe, K]]	+	[[Category: Tsunematsu Y]]
-	[[Category: Yamamoto, T]]	+	[[Category: Watanabe K]]
-	~~[[Category: Gst]]~~	+	[[Category: Yamamoto T]]
-	~~[[Category: Transferase~~]]	+

OCA at 07:55, 16 November 2017

OCA — Thu, 16 Nov 2017 07:55:50 GMT

←Older revision		Revision as of 07:55, 16 November 2017
Line 3:		Line 3:
	<StructureSection load='5f8b' size='340' side='right' caption='[[5f8b]], [[Resolution\|resolution]] 2.54Å' scene=''>		<StructureSection load='5f8b' size='340' side='right' caption='[[5f8b]], [[Resolution\|resolution]] 2.54Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5f8b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F8B FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5f8b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfu Aspfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F8B FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=PZS:(5~{S},8~{S},9~{R})-2-[(~{E})-HEX-1-ENYL]-8-METHOXY-3-METHYL-9-OXIDANYL-8-(PHENYLCARBONYL)-1-OXA-7-AZASPIRO[4.4]NON-2-ENE-4,6-DIONE'>PZS</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=PZS:(5~{S},8~{S},9~{R})-2-[(~{E})-HEX-1-ENYL]-8-METHOXY-3-METHYL-9-OXIDANYL-8-(PHENYLCARBONYL)-1-OXA-7-AZASPIRO[4.4]NON-2-ENE-4,6-DIONE'>PZS</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=5f8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8b OCA], [http://pdbe.org/5f8b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8b RCSB], [http://www.ebi.ac.uk/pdbsum/5f8b PDBsum]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AFUA_8G00580 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=330879 ASPFU])</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=5f8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8b OCA], [http://pdbe.org/5f8b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8b RCSB], [http://www.ebi.ac.uk/pdbsum/5f8b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8b ProSAT]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Geometric isomerization can expand the scope of biological activities of natural products. The observed chemical diversity among the pseurotin-type fungal secondary metabolites is in part generated by a trans to cis isomerization of an olefin. In vitro characterizations of pseurotin biosynthetic enzymes revealed that the glutathione S-transferase PsoE requires participation of the bifunctional C-methyltransferase/epoxidase PsoF to complete the trans to cis isomerization of the pathway intermediate presynerazol. The crystal structure of the PsoE/glutathione/presynerazol complex indicated stereospecific glutathione-presynerazol conjugate formation is the principal function of PsoE. Moreover, PsoF was identified to have an additional, unexpected oxidative isomerase activity, thus making it a trifunctional enzyme which is key to the complexity generation in pseurotin biosynthesis. Through the study, we identified a novel mechanism of accomplishing a seemingly simple trans to cis isomerization reaction.
		+
		+	Oxidative trans to cis Isomerization of Olefins in Polyketide Biosynthesis.,Yamamoto T, Tsunematsu Y, Hara K, Suzuki T, Kishimoto S, Kawagishi H, Noguchi H, Hashimoto H, Tang Y, Hotta K, Watanabe K Angew Chem Int Ed Engl. 2016 May 17;55(21):6207-10. doi: 10.1002/anie.201600940. , Epub 2016 Apr 13. PMID:27072782<ref>PMID:27072782</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5f8b" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Aspfu]]
	[[Category: Hara, K]]		[[Category: Hara, K]]
	[[Category: Hashimoto, H]]		[[Category: Hashimoto, H]]

OCA at 18:44, 12 May 2016

OCA — Thu, 12 May 2016 18:44:39 GMT

←Older revision		Revision as of 18:44, 12 May 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5f8b ~~is ON HOLD until Paper Publication~~	+	==Crystallographic Structure of PsoE with Co==
-		+	<StructureSection load='5f8b' size='340' side='right' caption='[[5f8b]], [[Resolution\|resolution]] 2.54Å' scene=''>
-	~~Authors~~: ~~Hara, K~~.~~, Hashimoto, H~~.~~, Yamamoto, T~~., ~~Tsunematsu~~, Y., ~~Watanabe~~, K.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5f8b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F8B FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=PZS:(5~{S},8~{S},9~{R})-2-[(~{E})-HEX-1-ENYL]-8-METHOXY-3-METHYL-9-OXIDANYL-8-(PHENYLCARBONYL)-1-OXA-7-AZASPIRO[4.4]NON-2-ENE-4,6-DIONE'>PZS</scene></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	<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=5f8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8b OCA], [http://pdbe.org/5f8b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8b RCSB], [http://www.ebi.ac.uk/pdbsum/5f8b PDBsum]</span></td></tr>
-	[[Category: ~~Yamamoto~~, T]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Hara, K]]
	[[Category: Hashimoto, H]]		[[Category: Hashimoto, H]]
		+	[[Category: Tsunematsu, Y]]
	[[Category: Watanabe, K]]		[[Category: Watanabe, K]]
-	[[Category: ~~Hara~~, K]]	+	[[Category: Yamamoto, T]]
-	[[Category: ~~Tsunematsu, Y~~]]	+	[[Category: Gst]]
		+	[[Category: Transferase]]

OCA at 17:58, 13 January 2016

OCA — Wed, 13 Jan 2016 17:58:39 GMT

←Older revision		Revision as of 17:58, 13 January 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5f8b is ON HOLD	+	The entry 5f8b is ON HOLD until Paper Publication

	Authors: Hara, K., Hashimoto, H., Yamamoto, T., Tsunematsu, Y., Watanabe, K.		Authors: Hara, K., Hashimoto, H., Yamamoto, T., Tsunematsu, Y., Watanabe, K.

OCA at 17:38, 30 December 2015

OCA — Wed, 30 Dec 2015 17:38:16 GMT

←Older revision		Revision as of 17:38, 30 December 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5f8b is ON HOLD ~~until Paper Publication~~	+	The entry 5f8b is ON HOLD

	Authors: Hara, K., Hashimoto, H., Yamamoto, T., Tsunematsu, Y., Watanabe, K.		Authors: Hara, K., Hashimoto, H., Yamamoto, T., Tsunematsu, Y., Watanabe, K.

OCA at 11:18, 23 December 2015

OCA — Wed, 23 Dec 2015 11:18:01 GMT

←Older revision		Revision as of 11:18, 23 December 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5f8b is ON HOLD	+	The entry 5f8b is ON HOLD until Paper Publication

	Authors: Hara, K., Hashimoto, H., Yamamoto, T., Tsunematsu, Y., Watanabe, K.		Authors: Hara, K., Hashimoto, H., Yamamoto, T., Tsunematsu, Y., Watanabe, K.

OCA: Protected "5f8b" [edit=sysop:move=sysop]

OCA — Wed, 16 Dec 2015 12:42:50 GMT

Protected "5f8b" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:42, 16 December 2015

OCA: New page: '''Unreleased structure''' The entry 5f8b is ON HOLD Authors: Hara, K., Hashimoto, H., Yamamoto, T., Tsunematsu, Y., Watanabe, K. Description: Category: Unreleased Structures [[Ca...

OCA — Wed, 16 Dec 2015 12:42:49 GMT

New page: '''Unreleased structure''' The entry 5f8b is ON HOLD Authors: Hara, K., Hashimoto, H., Yamamoto, T., Tsunematsu, Y., Watanabe, K. Description: Category: Unreleased Structures [[Ca...

New page

'''Unreleased structure'''

The entry 5f8b is ON HOLD

Authors: Hara, K., Hashimoto, H., Yamamoto, T., Tsunematsu, Y., Watanabe, K.

Description:
[[Category: Unreleased Structures]]
[[Category: Yamamoto, T]]
[[Category: Hashimoto, H]]
[[Category: Watanabe, K]]
[[Category: Hara, K]]
[[Category: Tsunematsu, Y]]