3vs8 - Revision history

OCA at 08:41, 20 March 2024

2024-03-20T08:41:39Z

←Older revision		Revision as of 08:41, 20 March 2024
Line 3:		Line 3:
	<StructureSection load='3vs8' size='340' side='right'caption='[[3vs8]], [[Resolution\|resolution]] 1.76Å' scene=''>		<StructureSection load='3vs8' size='340' side='right'caption='[[3vs8]], [[Resolution\|resolution]] 1.76Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3vs8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_478 Atcc 478~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VS8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3vs8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VS8 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.76Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[3vs9\|3vs9]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74]~~ </~~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=3vs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vs8 OCA], [https://pdbe.org/3vs8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vs8 RCSB], [https://www.ebi.ac.uk/pdbsum/3vs8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vs8 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=3vs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vs8 OCA], [https://pdbe.org/3vs8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vs8 RCSB], [https://www.ebi.ac.uk/pdbsum/3vs8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vs8 ProSAT]</span></td></tr>
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[https://www.uniprot.org/uniprot/C1DM33_AZOVD C1DM33_AZOVD]
-	Type III polyketide synthases (PKSs) show diverse cyclization specificity. We have previously characterized two Azotobacter type III PKSs (ArsB and ArsC) with different cyclization specificity. ArsB and ArsC, which share a high sequence identity (71%), produce alkylresorcinols and alkylpyrones, through aldol condensation and lactonization of the same polyketomethylene intermediate, respectively. Here we identified a key amino acid residue for the cyclization specificity of each enzyme by site-directed mutagenesis. Trp281 of ArsB corresponded to Gly284 of ArsC in the amino acid sequence alignment. The ArsB W281G mutant synthesized alkylpyrone, but not alkylresorcinol. In contrast, the ArsC G284W mutant synthesized alkylresorcinol with a small amount of alkylpyrone. These results indicate that this amino acid residue (Trp281 of ArsB or Gly284 of ArsC) should occupy a critical position for the cyclization specificity of each enzyme. We then determined crystal structures of the wild-type and G284W ArsC proteins at resolutions of 1.76 and 1.99 A, respectively. Comparison of these two ArsC structures indicates that the G284W substitution brings a steric wall to the active site cavity, resulting in a significant reduction of the cavity volume. We postulate that the polyketomethylene intermediate can be folded to a suitable form for aldol condensation only in such a relatively narrow cavity of ArsC G284W (and presumably ArsB). This is the first report on the alteration of cyclization specificity from lactonization to aldol condensation for a type III PKS. The ArsC G284W structure is significant as it is the first reported structure of a microbial resorcinol synthase.	+
-		+
-	~~Structural basis for cyclization specificity of two Azotobacter type III polyketide synthases~~: a single amino acid substitution reverses their cyclization specificity.,Satou R, Miyanaga A, Ozawa H, Funa N, Katsuyama Y, Miyazono KI, Tanokura M, Ohnishi Y, Horinouchi S J Biol Chem. 2013 Oct 7. PMID:24100027<ref>PMID:24100027</~~ref>~~	+
-		+
-	~~From MEDLINE®~~/~~PubMed®, a database of the U~~.S. ~~National Library of Medicine.<br>~~	+
-	</~~div>~~	+
-	~~<div class="pdbe-citations 3vs8" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references~~/>	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Atcc 478~~]]	+	[[Category: Azotobacter vinelandii]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Naringenin-chalcone synthase]]~~	+	[[Category: Funa N]]
-	[[Category: Funa, N]]	+	[[Category: Horinouchi S]]
-	[[Category: Horinouchi, S]]	+	[[Category: Miyanaga A]]
-	[[Category: Miyanaga, A]]	+	[[Category: Miyazono K]]
-	[[Category: Miyazono, K]]	+	[[Category: Ohnishi Y]]
-	[[Category: Ohnishi, Y]]	+	[[Category: Ozawa H]]
-	[[Category: Ozawa, H]]	+	[[Category: Satou R]]
-	[[Category: Satou, R]]	+	[[Category: Tanokura M]]
-	[[Category: Tanokura, M]]	+
-	~~[[Category: Condensing enzyme]]~~	+
-	~~[[Category: Thiolase fold]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 19:01, 27 July 2022

2022-07-27T19:01:15Z

←Older revision		Revision as of 19:01, 27 July 2022
Line 1:		Line 1:

	==Crystal structure of type III PKS ArsC==		==Crystal structure of type III PKS ArsC==
-	<StructureSection load='3vs8' size='340' side='right' caption='[[3vs8]], [[Resolution\|resolution]] 1.76Å' scene=''>	+	<StructureSection load='3vs8' size='340' side='right'caption='[[3vs8]], [[Resolution\|resolution]] 1.76Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3vs8]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3VS8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3vs8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VS8 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vs9\|3vs9]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vs9\|3vs9]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74] </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=3vs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vs8 OCA], [~~http~~://pdbe.org/3vs8 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3vs8 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3vs8 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3vs8 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=3vs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vs8 OCA], [https://pdbe.org/3vs8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vs8 RCSB], [https://www.ebi.ac.uk/pdbsum/3vs8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vs8 ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 478]]		[[Category: Atcc 478]]
		+	[[Category: Large Structures]]
	[[Category: Naringenin-chalcone synthase]]		[[Category: Naringenin-chalcone synthase]]
	[[Category: Funa, N]]		[[Category: Funa, N]]

OCA at 15:33, 11 August 2016

2016-08-11T15:33:12Z

←Older revision		Revision as of 15:33, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of type III PKS ArsC==		==Crystal structure of type III PKS ArsC==
	<StructureSection load='3vs8' size='340' side='right' caption='[[3vs8]], [[Resolution\|resolution]] 1.76Å' scene=''>		<StructureSection load='3vs8' size='340' side='right' caption='[[3vs8]], [[Resolution\|resolution]] 1.76Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vs9\|3vs9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vs9\|3vs9]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74] </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=3vs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vs8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vs8 RCSB], [http://www.ebi.ac.uk/pdbsum/3vs8 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=3vs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vs8 OCA], [http://pdbe.org/3vs8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vs8 RCSB], [http://www.ebi.ac.uk/pdbsum/3vs8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vs8 ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 16:		Line 17:
	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 3vs8" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:48, 4 January 2015

2015-01-04T10:48:23Z

←Older revision		Revision as of 10:48, 4 January 2015
Line 2:		Line 2:
	<StructureSection load='3vs8' size='340' side='right' caption='[[3vs8]], [[Resolution\|resolution]] 1.76Å' scene=''>		<StructureSection load='3vs8' size='340' side='right' caption='[[3vs8]], [[Resolution\|resolution]] 1.76Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3vs8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA]. <br>	+	<table><tr><td colspan='2'>[[3vs8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VS8 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vs9\|3vs9]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vs9\|3vs9]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Glucokinase Glucokinase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74] </span></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=3vs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vs8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vs8 RCSB], [http://www.ebi.ac.uk/pdbsum/3vs8 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=3vs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vs8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vs8 RCSB], [http://www.ebi.ac.uk/pdbsum/3vs8 PDBsum]</span></td></tr>
-	<table>	+	</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		Line 14:
	Structural basis for cyclization specificity of two Azotobacter type III polyketide synthases: a single amino acid substitution reverses their cyclization specificity.,Satou R, Miyanaga A, Ozawa H, Funa N, Katsuyama Y, Miyazono KI, Tanokura M, Ohnishi Y, Horinouchi S J Biol Chem. 2013 Oct 7. PMID:24100027<ref>PMID:24100027</ref>		Structural basis for cyclization specificity of two Azotobacter type III polyketide synthases: a single amino acid substitution reverses their cyclization specificity.,Satou R, Miyanaga A, Ozawa H, Funa N, Katsuyama Y, Miyazono KI, Tanokura M, Ohnishi Y, Horinouchi S J Biol Chem. 2013 Oct 7. PMID:24100027<ref>PMID:24100027</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
Line 22:		Line 22:
	[[Category: Atcc 478]]		[[Category: Atcc 478]]
	[[Category: Naringenin-chalcone synthase]]		[[Category: Naringenin-chalcone synthase]]
-	[[Category: Funa, N.]]	+	[[Category: Funa, N]]
-	[[Category: Horinouchi, S.]]	+	[[Category: Horinouchi, S]]
-	[[Category: Miyanaga, A.]]	+	[[Category: Miyanaga, A]]
-	[[Category: Miyazono, K.]]	+	[[Category: Miyazono, K]]
-	[[Category: Ohnishi, Y.]]	+	[[Category: Ohnishi, Y]]
-	[[Category: Ozawa, H.]]	+	[[Category: Ozawa, H]]
-	[[Category: Satou, R.]]	+	[[Category: Satou, R]]
-	[[Category: Tanokura, M.]]	+	[[Category: Tanokura, M]]
	[[Category: Condensing enzyme]]		[[Category: Condensing enzyme]]
	[[Category: Thiolase fold]]		[[Category: Thiolase fold]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 09:34, 1 May 2014

2014-05-01T09:34:46Z

←Older revision		Revision as of 09:34, 1 May 2014
Line 2:		Line 2:
	<StructureSection load='3vs8' size='340' side='right' caption='[[3vs8]], [[Resolution\|resolution]] 1.76Å' scene=''>		<StructureSection load='3vs8' size='340' side='right' caption='[[3vs8]], [[Resolution\|resolution]] 1.76Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	[[3vs8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA]. <br>	+	<table><tr><td colspan='2'>[[3vs8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA]. <br>
-	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>
-	<b>[[Related_structure\|Related:]]</b> [[3vs9\|3vs9]]<br>	+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vs9\|3vs9]]</td></tr>
-	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>	+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
-	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vs8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vs8 RCSB], [http://www.ebi.ac.uk/pdbsum/3vs8 PDBsum]</span><br>	+	<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=3vs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vs8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vs8 RCSB], [http://www.ebi.ac.uk/pdbsum/3vs8 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	Type III polyketide synthases (PKSs) show diverse cyclization specificity. We have previously characterized two Azotobacter type III PKSs (ArsB and ArsC) with different cyclization specificity. ArsB and ArsC, which share a high sequence identity (71%), produce alkylresorcinols and alkylpyrones, through aldol condensation and lactonization of the same polyketomethylene intermediate, respectively. Here we identified a key amino acid residue for the cyclization specificity of each enzyme by site-directed mutagenesis. Trp281 of ArsB corresponded to Gly284 of ArsC in the amino acid sequence alignment. The ArsB W281G mutant synthesized alkylpyrone, but not alkylresorcinol. In contrast, the ArsC G284W mutant synthesized alkylresorcinol with a small amount of alkylpyrone. These results indicate that this amino acid residue (Trp281 of ArsB or Gly284 of ArsC) should occupy a critical position for the cyclization specificity of each enzyme. We then determined crystal structures of the wild-type and G284W ArsC proteins at resolutions of 1.76 and 1.99 A, respectively. Comparison of these two ArsC structures indicates that the G284W substitution brings a steric wall to the active site cavity, resulting in a significant reduction of the cavity volume. We postulate that the polyketomethylene intermediate can be folded to a suitable form for aldol condensation only in such a relatively narrow cavity of ArsC G284W (and presumably ArsB). This is the first report on the alteration of cyclization specificity from lactonization to aldol condensation for a type III PKS. The ArsC G284W structure is significant as it is the first reported structure of a microbial resorcinol synthase.		Type III polyketide synthases (PKSs) show diverse cyclization specificity. We have previously characterized two Azotobacter type III PKSs (ArsB and ArsC) with different cyclization specificity. ArsB and ArsC, which share a high sequence identity (71%), produce alkylresorcinols and alkylpyrones, through aldol condensation and lactonization of the same polyketomethylene intermediate, respectively. Here we identified a key amino acid residue for the cyclization specificity of each enzyme by site-directed mutagenesis. Trp281 of ArsB corresponded to Gly284 of ArsC in the amino acid sequence alignment. The ArsB W281G mutant synthesized alkylpyrone, but not alkylresorcinol. In contrast, the ArsC G284W mutant synthesized alkylresorcinol with a small amount of alkylpyrone. These results indicate that this amino acid residue (Trp281 of ArsB or Gly284 of ArsC) should occupy a critical position for the cyclization specificity of each enzyme. We then determined crystal structures of the wild-type and G284W ArsC proteins at resolutions of 1.76 and 1.99 A, respectively. Comparison of these two ArsC structures indicates that the G284W substitution brings a steric wall to the active site cavity, resulting in a significant reduction of the cavity volume. We postulate that the polyketomethylene intermediate can be folded to a suitable form for aldol condensation only in such a relatively narrow cavity of ArsC G284W (and presumably ArsB). This is the first report on the alteration of cyclization specificity from lactonization to aldol condensation for a type III PKS. The ArsC G284W structure is significant as it is the first reported structure of a microbial resorcinol synthase.
Line 13:		Line 15:

	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:09, 30 April 2014

2014-04-30T10:09:29Z

←Older revision		Revision as of 10:09, 30 April 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	[[3vs8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA]. <br>		[[3vs8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA]. <br>
-	<b>Related:</b> [[3vs9\|3vs9]]<br>	+	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>
		+	<b>[[Related_structure\|Related:]]</b> [[3vs9\|3vs9]]<br>
	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>		<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vs8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vs8 RCSB], [http://www.ebi.ac.uk/pdbsum/3vs8 PDBsum]</span><br>
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	Type III polyketide synthases (PKSs) show diverse cyclization specificity. We have previously characterized two Azotobacter type III PKSs (ArsB and ArsC) with different cyclization specificity. ArsB and ArsC, which share a high sequence identity (71%), produce alkylresorcinols and alkylpyrones, through aldol condensation and lactonization of the same polyketomethylene intermediate, respectively. Here we identified a key amino acid residue for the cyclization specificity of each enzyme by site-directed mutagenesis. Trp281 of ArsB corresponded to Gly284 of ArsC in the amino acid sequence alignment. The ArsB W281G mutant synthesized alkylpyrone, but not alkylresorcinol. In contrast, the ArsC G284W mutant synthesized alkylresorcinol with a small amount of alkylpyrone. These results indicate that this amino acid residue (Trp281 of ArsB or Gly284 of ArsC) should occupy a critical position for the cyclization specificity of each enzyme. We then determined crystal structures of the wild-type and G284W ArsC proteins at resolutions of 1.76 and 1.99 A, respectively. Comparison of these two ArsC structures indicates that the G284W substitution brings a steric wall to the active site cavity, resulting in a significant reduction of the cavity volume. We postulate that the polyketomethylene intermediate can be folded to a suitable form for aldol condensation only in such a relatively narrow cavity of ArsC G284W (and presumably ArsB). This is the first report on the alteration of cyclization specificity from lactonization to aldol condensation for a type III PKS. The ArsC G284W structure is significant as it is the first reported structure of a microbial resorcinol synthase.		Type III polyketide synthases (PKSs) show diverse cyclization specificity. We have previously characterized two Azotobacter type III PKSs (ArsB and ArsC) with different cyclization specificity. ArsB and ArsC, which share a high sequence identity (71%), produce alkylresorcinols and alkylpyrones, through aldol condensation and lactonization of the same polyketomethylene intermediate, respectively. Here we identified a key amino acid residue for the cyclization specificity of each enzyme by site-directed mutagenesis. Trp281 of ArsB corresponded to Gly284 of ArsC in the amino acid sequence alignment. The ArsB W281G mutant synthesized alkylpyrone, but not alkylresorcinol. In contrast, the ArsC G284W mutant synthesized alkylresorcinol with a small amount of alkylpyrone. These results indicate that this amino acid residue (Trp281 of ArsB or Gly284 of ArsC) should occupy a critical position for the cyclization specificity of each enzyme. We then determined crystal structures of the wild-type and G284W ArsC proteins at resolutions of 1.76 and 1.99 A, respectively. Comparison of these two ArsC structures indicates that the G284W substitution brings a steric wall to the active site cavity, resulting in a significant reduction of the cavity volume. We postulate that the polyketomethylene intermediate can be folded to a suitable form for aldol condensation only in such a relatively narrow cavity of ArsC G284W (and presumably ArsB). This is the first report on the alteration of cyclization specificity from lactonization to aldol condensation for a type III PKS. The ArsC G284W structure is significant as it is the first reported structure of a microbial resorcinol synthase.

OCA at 05:32, 30 April 2014

2014-04-30T05:32:37Z

←Older revision		Revision as of 05:32, 30 April 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3vs8\| PDB~~=3vs8 \| ~~SCENE~~= }}	+	==Crystal structure of type III PKS ArsC==
-	===~~Crystal~~ structure of type III PKS ArsC~~===~~	+	<StructureSection load='3vs8' size='340' side='right' caption='[[3vs8]], [[Resolution\|resolution]] 1.76Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24100027}}~~	+	== Structural highlights ==
		+	[[3vs8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA]. <br>
		+	<b>Related:</b> [[3vs9\|3vs9]]<br>
		+	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	== Publication Abstract from PubMed ==
		+	Type III polyketide synthases (PKSs) show diverse cyclization specificity. We have previously characterized two Azotobacter type III PKSs (ArsB and ArsC) with different cyclization specificity. ArsB and ArsC, which share a high sequence identity (71%), produce alkylresorcinols and alkylpyrones, through aldol condensation and lactonization of the same polyketomethylene intermediate, respectively. Here we identified a key amino acid residue for the cyclization specificity of each enzyme by site-directed mutagenesis. Trp281 of ArsB corresponded to Gly284 of ArsC in the amino acid sequence alignment. The ArsB W281G mutant synthesized alkylpyrone, but not alkylresorcinol. In contrast, the ArsC G284W mutant synthesized alkylresorcinol with a small amount of alkylpyrone. These results indicate that this amino acid residue (Trp281 of ArsB or Gly284 of ArsC) should occupy a critical position for the cyclization specificity of each enzyme. We then determined crystal structures of the wild-type and G284W ArsC proteins at resolutions of 1.76 and 1.99 A, respectively. Comparison of these two ArsC structures indicates that the G284W substitution brings a steric wall to the active site cavity, resulting in a significant reduction of the cavity volume. We postulate that the polyketomethylene intermediate can be folded to a suitable form for aldol condensation only in such a relatively narrow cavity of ArsC G284W (and presumably ArsB). This is the first report on the alteration of cyclization specificity from lactonization to aldol condensation for a type III PKS. The ArsC G284W structure is significant as it is the first reported structure of a microbial resorcinol synthase.

-	~~==About this Structure==~~	+	Structural basis for cyclization specificity of two Azotobacter type III polyketide synthases: a single amino acid substitution reverses their cyclization specificity.,Satou R, Miyanaga A, Ozawa H, Funa N, Katsuyama Y, Miyazono KI, Tanokura M, Ohnishi Y, Horinouchi S J Biol Chem. 2013 Oct 7. PMID:24100027<ref>PMID:24100027</ref>
-	~~[[3vs8]] is~~ a ~~8 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]~~. ~~Full crystallographic information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024100027</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	== References ==
-	[[Category: ~~Azotobacter vinelandii~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Atcc 478]]
	[[Category: Naringenin-chalcone synthase]]		[[Category: Naringenin-chalcone synthase]]
	[[Category: Funa, N.]]		[[Category: Funa, N.]]

OCA at 05:12, 23 October 2013

2013-10-23T05:12:59Z

←Older revision		Revision as of 05:12, 23 October 2013
Line 1:		Line 1:
	{{STRUCTURE_3vs8\| PDB=3vs8 \| SCENE= }}		{{STRUCTURE_3vs8\| PDB=3vs8 \| SCENE= }}
	===Crystal structure of type III PKS ArsC===		===Crystal structure of type III PKS ArsC===
		+	{{ABSTRACT_PUBMED_24100027}}

	==About this Structure==		==About this Structure==
	[[3vs8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA].		[[3vs8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:024100027</ref><references group="xtra"/><references/>
	[[Category: Azotobacter vinelandii]]		[[Category: Azotobacter vinelandii]]
	[[Category: Naringenin-chalcone synthase]]		[[Category: Naringenin-chalcone synthase]]

OCA at 11:24, 24 April 2013

2013-04-24T11:24:42Z

←Older revision		Revision as of 11:24, 24 April 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_3vs8\| PDB=3vs8 \| SCENE= }}
		+	===Crystal structure of type III PKS ArsC===

-	~~The entry~~ 3vs8 is ~~ON HOLD until Apr 23 2014~~	+	==About this Structure==
-		+	[[3vs8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VS8 OCA].
-	~~Authors~~: ~~Satou~~, R., Miyanaga, A.~~, Ozawa, H., Funa, N.,~~ Miyazono, K.~~, Tanokura, M.,~~ Ohnishi, Y., ~~Horinouchi~~, S.	+	[[Category: Azotobacter vinelandii]]
-		+	[[Category: Naringenin-chalcone synthase]]
-	~~Description~~: ~~Crystal structure of type III PKS ArsC~~	+	[[Category: Funa, N.]]
		+	[[Category: Horinouchi, S.]]
		+	[[Category: Miyanaga, A.]]
		+	[[Category: Miyazono, K.]]
		+	[[Category: Ohnishi, Y.]]
		+	[[Category: Ozawa, H.]]
		+	[[Category: Satou, R.]]
		+	[[Category: Tanokura, M.]]
		+	[[Category: Condensing enzyme]]
		+	[[Category: Thiolase fold]]
		+	[[Category: Transferase]]

OCA at 05:29, 23 May 2012

2012-05-23T05:29:56Z

←Older revision		Revision as of 05:29, 23 May 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3vs8 is ON HOLD	+	The entry 3vs8 is ON HOLD until Apr 23 2014

	Authors: Satou, R., Miyanaga, A., Ozawa, H., Funa, N., Miyazono, K., Tanokura, M., Ohnishi, Y., Horinouchi, S.		Authors: Satou, R., Miyanaga, A., Ozawa, H., Funa, N., Miyazono, K., Tanokura, M., Ohnishi, Y., Horinouchi, S.

	Description: Crystal structure of type III PKS ArsC		Description: Crystal structure of type III PKS ArsC