5xtn - Revision history

OCA at 08:13, 22 November 2023

2023-11-22T08:13:47Z

←Older revision		Revision as of 08:13, 22 November 2023
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	<StructureSection load='5xtn' size='340' side='right'caption='[[5xtn]], [[Resolution\|resolution]] 2.54Å' scene=''>		<StructureSection load='5xtn' size='340' side='right'caption='[[5xtn]], [[Resolution\|resolution]] 2.54Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xtn]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Acmnpv Acmnpv~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5XTN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xtn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Autographa_californica_nucleopolyhedrovirus Autographa californica nucleopolyhedrovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XTN FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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">P33, ORF92 ([http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=46015 AcMNPV])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[http://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2]~~ </~~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=5xtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xtn OCA], [https://pdbe.org/5xtn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xtn RCSB], [https://www.ebi.ac.uk/pdbsum/5xtn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xtn ProSAT]</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=5xtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xtn OCA], [~~http~~://pdbe.org/5xtn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5xtn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5xtn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5xtn ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FLSO_NPVAC FLSO_NPVAC]] Functional FAD-linked sulfhydryl oxidase that is required for infectious budded virion (BV) production and for the formation of enveloped occluded virion (ODV).<ref>PMID:19409596</ref>	+	[https://www.uniprot.org/uniprot/FLSO_NPVAC FLSO_NPVAC] Functional FAD-linked sulfhydryl oxidase that is required for infectious budded virion (BV) production and for the formation of enveloped occluded virion (ODV).<ref>PMID:19409596</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	==See Also==		==See Also==
-	*[[Sulfhydryl oxidase\|Sulfhydryl oxidase]]	+	*[[Sulfhydryl oxidase 3D structures\|Sulfhydryl oxidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Acmnpv~~]]	+	[[Category: Autographa californica nucleopolyhedrovirus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Thiol oxidase]]~~	+	[[Category: Gong P]]
-	[[Category: Gong, P]]	+	[[Category: Hu Z]]
-	[[Category: Hu, Z]]	+	[[Category: Kuang W]]
-	[[Category: Kuang, W]]	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Sulfhydryl oxidase~~]]	+

OCA at 12:41, 25 December 2019

2019-12-25T12:41:32Z

←Older revision		Revision as of 12:41, 25 December 2019
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	==Crystal structure of baculoviral sulfhydryl oxidase P33 (C155A, C158A mutant)==		==Crystal structure of baculoviral sulfhydryl oxidase P33 (C155A, C158A mutant)==
-	<StructureSection load='5xtn' size='340' side='right' caption='[[5xtn]], [[Resolution\|resolution]] 2.54Å' scene=''>	+	<StructureSection load='5xtn' size='340' side='right'caption='[[5xtn]], [[Resolution\|resolution]] 2.54Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5xtn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Acmnpv Acmnpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XTN FirstGlance]. <br>		<table><tr><td colspan='2'>[[5xtn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Acmnpv Acmnpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XTN FirstGlance]. <br>
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	</div>		</div>
	<div class="pdbe-citations 5xtn" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5xtn" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Sulfhydryl oxidase\|Sulfhydryl oxidase]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Acmnpv]]		[[Category: Acmnpv]]
		+	[[Category: Large Structures]]
	[[Category: Thiol oxidase]]		[[Category: Thiol oxidase]]
	[[Category: Gong, P]]		[[Category: Gong, P]]

OCA at 10:33, 22 November 2017

2017-11-22T10:33:19Z

←Older revision		Revision as of 10:33, 22 November 2017
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	<StructureSection load='5xtn' size='340' side='right' caption='[[5xtn]], [[Resolution\|resolution]] 2.54Å' scene=''>		<StructureSection load='5xtn' size='340' side='right' caption='[[5xtn]], [[Resolution\|resolution]] 2.54Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xtn]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XTN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xtn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Acmnpv Acmnpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XTN FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P33, ORF92 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46015 AcMNPV])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </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=5xtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xtn OCA], [http://pdbe.org/5xtn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xtn RCSB], [http://www.ebi.ac.uk/pdbsum/5xtn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xtn ProSAT]</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=5xtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xtn OCA], [http://pdbe.org/5xtn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xtn RCSB], [http://www.ebi.ac.uk/pdbsum/5xtn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xtn ProSAT]</span></td></tr>
Line 10:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/FLSO_NPVAC FLSO_NPVAC]] Functional FAD-linked sulfhydryl oxidase that is required for infectious budded virion (BV) production and for the formation of enveloped occluded virion (ODV).<ref>PMID:19409596</ref>		[[http://www.uniprot.org/uniprot/FLSO_NPVAC FLSO_NPVAC]] Functional FAD-linked sulfhydryl oxidase that is required for infectious budded virion (BV) production and for the formation of enveloped occluded virion (ODV).<ref>PMID:19409596</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Baculoviruses encode a conserved sulfhydryl oxidase, P33, which is necessary for budded virus (BV) production and multinucleocapsid occlusion-derived virus (ODV) formation. Here, the structural and functional relationship of P33 was revealed by X-ray crystallography, site-directed mutagenesis, and functional analysis. Based on crystallographic characterization and structural analysis, a series of P33 mutants within three conserved regions, i.e., the active site, the dimer interface, and the R127-E183 salt bridge, were constructed. In vitro experiments showed that mutations within the active site and dimer interface severely impaired the sulfhydryl oxidase activity of P33, while the mutations in the salt bridge had a relatively minor influence. Recombinant viruses containing mutated P33 were constructed and assayed in vivo Except for the active-site mutant AXXA, all other mutants produced infectious BVs, although certain mutants had a decreased BV production. The active-site mutant H114A, the dimer interface mutant H227D, and the salt bridge mutant R127A-E183A were further analyzed by electron microscopy and bioassays. The occlusion bodies (OBs) of mutants H114A and R127A-E183A had a ragged surface and contained mostly ODVs with a single nucleocapsid. The OBs of all three mutants contained lower numbers of ODVs and had a significantly reduced oral infectivity in comparison to control virus. Crystallographic analyses further revealed that all three regions may coordinate with one another to achieve optimal function of P33. Taken together, our data revealed that all the three conserved regions are involved in P33 activity and are crucial for virus morphogenesis and peroral infectivity.IMPORTANCE Sulfhydryl oxidase catalyzes disulfide bond formation of substrate proteins. P33, a baculovirus-encoded sulfhydryl oxidase, is different from other cellular and viral sulfhydryl oxidases, bearing unique features in tertiary and quaternary structure organizations. In this study, we found that three conserved regions, i.e., the active site, dimer interface, and the R127-E183 salt bridge, play important roles in the enzymatic activity and function of P33. Previous observations showed that deletion of p33 results in a total loss of budded virus (BV) production and in morphological changes in occlusion-derived virus (ODV). Our study revealed that certain P33 mutants lead to occlusion bodies (OBs) with a ragged surface, decreased embedded ODVs, and reduced oral infectivity. Interestingly, some P33 mutants with impaired ODV/OB still retained BV productivity, indicating that the impacts on BV and on ODV/OB are two distinctly different functions of P33, which are likely to be performed via different substrate proteins.
		+
		+	Three Conserved Regions in Baculovirus Sulfhydryl Oxidase P33 Are Critical for Enzymatic Activity and Function.,Kuang W, Zhang H, Wang M, Zhou NY, Deng F, Wang H, Gong P, Hu Z J Virol. 2017 Nov 14;91(23). pii: e01158-17. doi: 10.1128/JVI.01158-17. Print, 2017 Dec 1. PMID:28904203<ref>PMID:28904203</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5xtn" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Acmnpv]]
	[[Category: Thiol oxidase]]		[[Category: Thiol oxidase]]
	[[Category: Gong, P]]		[[Category: Gong, P]]

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

2017-10-06T05:35:09Z

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

←Older revision

Revision as of 05:35, 6 October 2017

OCA: New page: ==Crystal structure of baculoviral sulfhydryl oxidase P33 (C155A, C158A mutant)== == Structural highlights ==
<table><tr><td colspan='2'>[[5xtn]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTN OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XTN FirstGlance]. 
</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[http://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </td></tr>
<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xtn OCA], [http://pdbe.org/5xtn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xtn RCSB], [http://www.ebi.ac.uk/pdbsum/5xtn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xtn ProSAT]</td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/FLSO_NPVAC FLSO_NPVAC]] Functional FAD-linked sulfhydryl oxidase that is required for infectious budded virion (BV) production and for the formation of enveloped occluded virion (ODV).<ref>PMID:19409596</ref>
== References ==
<references/>
TOC
</StructureSection>
[[Category: Thiol oxidase]]
[[Category: Gong, P]]
[[Category: Hu, Z]]
[[Category: Kuang, W]]
[[Category: Oxidoreductase]]
[[Category: Sulfhydryl oxidase]]