2le2 - Revision history

OCA at 05:42, 15 May 2024

OCA — Wed, 15 May 2024 05:42:04 GMT

←Older revision		Revision as of 05:42, 15 May 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2le2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_phi29 Bacillus virus phi29]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LE2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2le2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_phi29 Bacillus virus phi29]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LE2 FirstGlance]. <br>
-	</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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [https://pdbe.org/2le2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [https://www.ebi.ac.uk/pdbsum/2le2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2le2 ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [https://pdbe.org/2le2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [https://www.ebi.ac.uk/pdbsum/2le2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2le2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 10:54, 15 February 2023

OCA — Wed, 15 Feb 2023 10:54:35 GMT

←Older revision		Revision as of 10:54, 15 February 2023
Line 1:		Line 1:

	==Novel dimeric structure of phage phi29-encoded protein p56: Insights into Uracil-DNA glycosylase inhibition==		==Novel dimeric structure of phage phi29-encoded protein p56: Insights into Uracil-DNA glycosylase inhibition==
-	<StructureSection load='2le2' size='340' side='right'caption='[[2le2~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2le2' size='340' side='right'caption='[[2le2]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2le2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Bpph2 Bpph2~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LE2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2le2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_phi29 Bacillus virus phi29]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LE2 FirstGlance]. <br>
-	</td></tr>~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">0.8 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 BPPH2])</td></tr>~~	+	</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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [https://pdbe.org/2le2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [https://www.ebi.ac.uk/pdbsum/2le2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2le2 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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [https://pdbe.org/2le2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [https://www.ebi.ac.uk/pdbsum/2le2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2le2 ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/P56_BPPH2 P56_BPPH2] Inhibits the host uracil-DNA glycosylase (UDG), an enzyme which removes uracil residues from DNA by the base excision repair. Interacts with host uracil-DNA glycosylase and prevents the latter from binding to DNA. Since the viral DNA polymerase efficiently incorporates dUMP into DNA, the virus needs to prevent the deleterious effect caused by host UDG when it eliminates uracil residues present in the viral genome.<ref>PMID:17698500</ref> <ref>PMID:18845683</ref> <ref>PMID:21542855</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bpph2~~]]	+	[[Category: Bacillus virus phi29]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Asensio, J]]	+	[[Category: Asensio J]]
-	[[Category: Gonzalez, C]]	+	[[Category: Gonzalez C]]
-	[[Category: Lazaro~~, J M~~]]	+	[[Category: Lazaro JM]]
-	[[Category: Perez-Lago, L]]	+	[[Category: Perez-Lago L]]
-	[[Category: Salas, M]]	+	[[Category: Salas M]]
-	[[Category: Serrano-Heras, G]]	+	[[Category: Serrano-Heras G]]
-	~~[[Category: Dna mimicry]]~~	+
-	~~[[Category: Dna repair inhibition]]~~	+
-	~~[[Category: Hydrolase inhibitor]]~~	+
-	~~[[Category: Udg inhibition~~]]	+

OCA at 10:08, 12 May 2021

OCA — Wed, 12 May 2021 10:08:58 GMT

←Older revision		Revision as of 10:08, 12 May 2021
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	==Novel dimeric structure of phage phi29-encoded protein p56: Insights into Uracil-DNA glycosylase inhibition==		==Novel dimeric structure of phage phi29-encoded protein p56: Insights into Uracil-DNA glycosylase inhibition==
-	<StructureSection load='2le2' size='340' side='right' caption='[[2le2]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2le2' size='340' side='right'caption='[[2le2]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2le2]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bpph2 Bpph2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2LE2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2le2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpph2 Bpph2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LE2 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">0.8 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 BPPH2])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">0.8 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 BPPH2])</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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [~~http~~://pdbe.org/2le2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2le2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2le2 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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [https://pdbe.org/2le2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [https://www.ebi.ac.uk/pdbsum/2le2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2le2 ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 21:		Line 21:
	</StructureSection>		</StructureSection>
	[[Category: Bpph2]]		[[Category: Bpph2]]
		+	[[Category: Large Structures]]
	[[Category: Asensio, J]]		[[Category: Asensio, J]]
	[[Category: Gonzalez, C]]		[[Category: Gonzalez, C]]

OCA at 19:39, 1 August 2018

OCA — Wed, 01 Aug 2018 19:39:34 GMT

←Older revision		Revision as of 19:39, 1 August 2018
Line 1:		Line 1:
		+
	==Novel dimeric structure of phage phi29-encoded protein p56: Insights into Uracil-DNA glycosylase inhibition==		==Novel dimeric structure of phage phi29-encoded protein p56: Insights into Uracil-DNA glycosylase inhibition==
	<StructureSection load='2le2' size='340' side='right' caption='[[2le2]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2le2' size='340' side='right' caption='[[2le2]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[2le2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpph2 Bpph2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LE2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2le2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpph2 Bpph2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LE2 FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">0.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 BPPH2])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">0.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 BPPH2])</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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [http://pdbe.org/2le2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [http://www.ebi.ac.uk/pdbsum/2le2 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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [http://pdbe.org/2le2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [http://www.ebi.ac.uk/pdbsum/2le2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2le2 ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 20:56, 10 September 2015

OCA — Thu, 10 Sep 2015 20:56:23 GMT

←Older revision		Revision as of 20:56, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='2le2' size='340' side='right' caption='[[2le2]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2le2' size='340' side='right' caption='[[2le2]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2le2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bacillus_phage_phi29 Bacillus phage phi29~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LE2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2le2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpph2 Bpph2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LE2 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">0.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 ~~Bacillus phage phi29~~])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">0.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 BPPH2])</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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [http://www.ebi.ac.uk/pdbsum/2le2 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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [http://pdbe.org/2le2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [http://www.ebi.ac.uk/pdbsum/2le2 PDBsum]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	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 2le2" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus phage phi29~~]]	+	[[Category: Bpph2]]
	[[Category: Asensio, J]]		[[Category: Asensio, J]]
	[[Category: Gonzalez, C]]		[[Category: Gonzalez, C]]

OCA at 05:22, 22 December 2014

OCA — Mon, 22 Dec 2014 05:22:56 GMT

←Older revision		Revision as of 05:22, 22 December 2014
Line 2:		Line 2:
	<StructureSection load='2le2' size='340' side='right' caption='[[2le2]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2le2' size='340' side='right' caption='[[2le2]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2le2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_phi29 Bacillus phage phi29]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. <br>	+	<table><tr><td colspan='2'>[[2le2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_phi29 Bacillus phage phi29]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LE2 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">0.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 Bacillus phage phi29])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">0.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 Bacillus phage phi29])</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='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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [http://www.ebi.ac.uk/pdbsum/2le2 PDBsum]</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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [http://www.ebi.ac.uk/pdbsum/2le2 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 13:		Line 12:
	Novel dimeric structure of phage {phi}29-encoded protein p56: insights into uracil-DNA glycosylase inhibition.,Asensio JL, Perez-Lago L, Lazaro JM, Gonzalez C, Serrano-Heras G, Salas M Nucleic Acids Res. 2011 Sep 2. PMID:21890898<ref>PMID:21890898</ref>		Novel dimeric structure of phage {phi}29-encoded protein p56: insights into uracil-DNA glycosylase inhibition.,Asensio JL, Perez-Lago L, Lazaro JM, Gonzalez C, Serrano-Heras G, Salas M Nucleic Acids Res. 2011 Sep 2. PMID:21890898<ref>PMID:21890898</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 20:		Line 19:
	</StructureSection>		</StructureSection>
	[[Category: Bacillus phage phi29]]		[[Category: Bacillus phage phi29]]
-	[[Category: Asensio, J.]]	+	[[Category: Asensio, J]]
-	[[Category: Gonzalez, C.]]	+	[[Category: Gonzalez, C]]
-	[[Category: Lazaro, J M.]]	+	[[Category: Lazaro, J M]]
-	[[Category: Perez-Lago, L.]]	+	[[Category: Perez-Lago, L]]
-	[[Category: Salas, M.]]	+	[[Category: Salas, M]]
-	[[Category: Serrano-Heras, G.]]	+	[[Category: Serrano-Heras, G]]
	[[Category: Dna mimicry]]		[[Category: Dna mimicry]]
	[[Category: Dna repair inhibition]]		[[Category: Dna repair inhibition]]
	[[Category: Hydrolase inhibitor]]		[[Category: Hydrolase inhibitor]]
	[[Category: Udg inhibition]]		[[Category: Udg inhibition]]

OCA at 10:00, 1 May 2014

OCA — Thu, 01 May 2014 10:00:31 GMT

←Older revision		Revision as of 10:00, 1 May 2014
Line 2:		Line 2:
	<StructureSection load='2le2' size='340' side='right' caption='[[2le2]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2le2' size='340' side='right' caption='[[2le2]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	[[2le2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_phi29 Bacillus phage phi29]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. <br>	+	<table><tr><td colspan='2'>[[2le2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_phi29 Bacillus phage phi29]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. <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>	+	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">0.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 Bacillus phage phi29])</td></tr>
-	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [http://www.ebi.ac.uk/pdbsum/2le2 PDBsum]</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>
		+	<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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [http://www.ebi.ac.uk/pdbsum/2le2 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	Protein p56 encoded by the Bacillus subtilis phage 29 inhibits the host uracil-DNA glycosylase (UDG) activity. To get insights into the structural basis for this inhibition, the NMR solution structure of p56 has been determined. The inhibitor defines a novel dimeric fold, stabilized by a combination of polar and extensive hydrophobic interactions. Each polypeptide chain contains three stretches of anti-parallel beta-sheets and a helical region linked by three short loops. In addition, microcalorimetry titration experiments showed that it forms a tight 2:1 complex with UDG, strongly suggesting that the dimer represents the functional form of the inhibitor. This was further confirmed by the functional analysis of p56 mutants unable to assemble into dimers. We have also shown that the highly anionic region of the inhibitor plays a significant role in the inhibition of UDG. Thus, based on these findings and taking into account previous results that revealed similarities between the association mode of p56 and the phage PBS-1/PBS-2-encoded inhibitor Ugi with UDG, we propose that protein p56 might inhibit the enzyme by mimicking its DNA substrate.		Protein p56 encoded by the Bacillus subtilis phage 29 inhibits the host uracil-DNA glycosylase (UDG) activity. To get insights into the structural basis for this inhibition, the NMR solution structure of p56 has been determined. The inhibitor defines a novel dimeric fold, stabilized by a combination of polar and extensive hydrophobic interactions. Each polypeptide chain contains three stretches of anti-parallel beta-sheets and a helical region linked by three short loops. In addition, microcalorimetry titration experiments showed that it forms a tight 2:1 complex with UDG, strongly suggesting that the dimer represents the functional form of the inhibitor. This was further confirmed by the functional analysis of p56 mutants unable to assemble into dimers. We have also shown that the highly anionic region of the inhibitor plays a significant role in the inhibition of UDG. Thus, based on these findings and taking into account previous results that revealed similarities between the association mode of p56 and the phage PBS-1/PBS-2-encoded inhibitor Ugi with UDG, we propose that protein p56 might inhibit the enzyme by mimicking its DNA substrate.
Line 11:		Line 14:

	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 10:26, 30 April 2014

OCA — Wed, 30 Apr 2014 10:26:01 GMT

←Older revision		Revision as of 10:26, 30 April 2014
Line 4:		Line 4:
	[[2le2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_phi29 Bacillus phage phi29]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. <br>		[[2le2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_phi29 Bacillus phage phi29]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. <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=2le2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2le2 RCSB], [http://www.ebi.ac.uk/pdbsum/2le2 PDBsum]</span><br>
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	Protein p56 encoded by the Bacillus subtilis phage 29 inhibits the host uracil-DNA glycosylase (UDG) activity. To get insights into the structural basis for this inhibition, the NMR solution structure of p56 has been determined. The inhibitor defines a novel dimeric fold, stabilized by a combination of polar and extensive hydrophobic interactions. Each polypeptide chain contains three stretches of anti-parallel beta-sheets and a helical region linked by three short loops. In addition, microcalorimetry titration experiments showed that it forms a tight 2:1 complex with UDG, strongly suggesting that the dimer represents the functional form of the inhibitor. This was further confirmed by the functional analysis of p56 mutants unable to assemble into dimers. We have also shown that the highly anionic region of the inhibitor plays a significant role in the inhibition of UDG. Thus, based on these findings and taking into account previous results that revealed similarities between the association mode of p56 and the phage PBS-1/PBS-2-encoded inhibitor Ugi with UDG, we propose that protein p56 might inhibit the enzyme by mimicking its DNA substrate.		Protein p56 encoded by the Bacillus subtilis phage 29 inhibits the host uracil-DNA glycosylase (UDG) activity. To get insights into the structural basis for this inhibition, the NMR solution structure of p56 has been determined. The inhibitor defines a novel dimeric fold, stabilized by a combination of polar and extensive hydrophobic interactions. Each polypeptide chain contains three stretches of anti-parallel beta-sheets and a helical region linked by three short loops. In addition, microcalorimetry titration experiments showed that it forms a tight 2:1 complex with UDG, strongly suggesting that the dimer represents the functional form of the inhibitor. This was further confirmed by the functional analysis of p56 mutants unable to assemble into dimers. We have also shown that the highly anionic region of the inhibitor plays a significant role in the inhibition of UDG. Thus, based on these findings and taking into account previous results that revealed similarities between the association mode of p56 and the phage PBS-1/PBS-2-encoded inhibitor Ugi with UDG, we propose that protein p56 might inhibit the enzyme by mimicking its DNA substrate.

OCA at 08:43, 30 April 2014

OCA — Wed, 30 Apr 2014 08:43:05 GMT

←Older revision		Revision as of 08:43, 30 April 2014
Line 1:		Line 1:
-	[[~~Image:~~2le2~~.png~~\|~~left\|200px~~]]	+	==Novel dimeric structure of phage phi29-encoded protein p56: Insights into Uracil-DNA glycosylase inhibition==
		+	<StructureSection load='2le2' size='340' side='right' caption='[[2le2]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	[[2le2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_phi29 Bacillus phage phi29]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA]. <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 ==
		+	Protein p56 encoded by the Bacillus subtilis phage 29 inhibits the host uracil-DNA glycosylase (UDG) activity. To get insights into the structural basis for this inhibition, the NMR solution structure of p56 has been determined. The inhibitor defines a novel dimeric fold, stabilized by a combination of polar and extensive hydrophobic interactions. Each polypeptide chain contains three stretches of anti-parallel beta-sheets and a helical region linked by three short loops. In addition, microcalorimetry titration experiments showed that it forms a tight 2:1 complex with UDG, strongly suggesting that the dimer represents the functional form of the inhibitor. This was further confirmed by the functional analysis of p56 mutants unable to assemble into dimers. We have also shown that the highly anionic region of the inhibitor plays a significant role in the inhibition of UDG. Thus, based on these findings and taking into account previous results that revealed similarities between the association mode of p56 and the phage PBS-1/PBS-2-encoded inhibitor Ugi with UDG, we propose that protein p56 might inhibit the enzyme by mimicking its DNA substrate.

-	<!--	+	Novel dimeric structure of phage {phi}29-encoded protein p56: insights into uracil-DNA glycosylase inhibition.,Asensio JL, Perez-Lago L, Lazaro JM, Gonzalez C, Serrano-Heras G, Salas M Nucleic Acids Res. 2011 Sep 2. PMID:21890898<ref>PMID:21890898</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_2le2"~~, ~~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_2le2\| PDB=2le2 \| SCENE= }}~~	+

-	~~===Novel dimeric structure~~ of ~~phage phi29-encoded protein p56: Insights into Uracil-DNA glycosylase inhibition===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	== References ==
-		+	<references/>
-	~~<!--~~	+	__TOC__
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_21890898}}, adds~~ the ~~Publication Abstract to the page~~	+	</StructureSection>
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 21890898 is the PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_21890898}}~~	+
-		+
-	==~~About this Structure~~==	+
-	~~[[2le2]] is a 2 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Bacillus_phage_phi29 Bacillus phage phi29]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE2 OCA].~~	+
-		+
-	~~==Reference==~~	+
-	<~~ref group="xtra">PMID:021890898</ref><references group="xtra"~~/>	+
	[[Category: Bacillus phage phi29]]		[[Category: Bacillus phage phi29]]
	[[Category: Asensio, J.]]		[[Category: Asensio, J.]]

OCA at 08:16, 30 October 2011

OCA — Sun, 30 Oct 2011 08:16:52 GMT

←Older revision		Revision as of 08:16, 30 October 2011
Line 1:		Line 1:
-	[[Image:2le2.~~jpg~~\|left\|200px]]	+	[[Image:2le2.png\|left\|200px]]

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