4kg3 - Revision history

OCA at 12:12, 1 March 2024

OCA — Fri, 01 Mar 2024 12:12:42 GMT

←Older revision		Revision as of 12:12, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4kg3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KG3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4kg3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KG3 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.7Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4kg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kg3 OCA], [https://pdbe.org/4kg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kg3 RCSB], [https://www.ebi.ac.uk/pdbsum/4kg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kg3 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=4kg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kg3 OCA], [https://pdbe.org/4kg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kg3 RCSB], [https://www.ebi.ac.uk/pdbsum/4kg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kg3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DCP2_YEAST DCP2_YEAST] Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.<ref>PMID:10508173</ref> <ref>PMID:11139489</ref> <ref>PMID:11741542</ref> <ref>PMID:12554866</ref>		[https://www.uniprot.org/uniprot/DCP2_YEAST DCP2_YEAST] Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.<ref>PMID:10508173</ref> <ref>PMID:11139489</ref> <ref>PMID:11741542</ref> <ref>PMID:12554866</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Removal of the 5' cap structure by Dcp2 is a major step in several 5'-3' mRNA decay pathways. The activity of Dcp2 is enhanced by Dcp1 and bound coactivators, yet the details of how these interactions are linked to chemistry are poorly understood. Here, we report three crystal structures of the catalytic Nudix hydrolase domain of Dcp2 that demonstrate binding of a catalytically essential metal ion, and enzyme kinetics are used to identify several key active site residues involved in acid/base chemistry of decapping. Using nuclear magnetic resonance and molecular dynamics, we find that a conserved metal binding loop on the catalytic domain undergoes conformational changes during the catalytic cycle. These findings describe key events during the chemical step of decapping, suggest local active site conformational changes are important for activity, and provide a framework to explain stimulation of catalysis by the regulatory domain of Dcp2 and associated coactivators.
-
-	Active Site Conformational Dynamics Are Coupled to Catalysis in the mRNA Decapping Enzyme Dcp2.,Aglietti RA, Floor SN, McClendon CL, Jacobson MP, Gross JD Structure. 2013 Jul 31. pii: S0969-2126(13)00245-1. doi:, 10.1016/j.str.2013.06.021. PMID:23911090<ref>PMID:23911090</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4kg3" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:56, 30 November 2022

OCA — Wed, 30 Nov 2022 11:56:46 GMT

←Older revision		Revision as of 11:56, 30 November 2022
Line 1:		Line 1:

	==Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain in complex with Mg (E153Q mutation)==		==Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain in complex with Mg (E153Q mutation)==
-	<StructureSection load='4kg3' size='340' side='right' caption='[[4kg3]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='4kg3' size='340' side='right'caption='[[4kg3]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4kg3]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Baker's_yeast Baker's yeast~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KG3 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4KG3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4kg3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KG3 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4k6e\|4k6e]], [[4kg4\|4kg4]]</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=4kg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kg3 OCA], [https://pdbe.org/4kg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kg3 RCSB], [https://www.ebi.ac.uk/pdbsum/4kg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kg3 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DCP2, N1917, PSU1, YNL118C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=4kg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kg3 OCA], [~~http~~://pdbe.org/4kg3 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4kg3 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4kg3 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4kg3 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DCP2_YEAST DCP2_YEAST]] Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.<ref>PMID:10508173</ref> <ref>PMID:11139489</ref> <ref>PMID:11741542</ref> <ref>PMID:12554866</ref>	+	[https://www.uniprot.org/uniprot/DCP2_YEAST DCP2_YEAST] Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.<ref>PMID:10508173</ref> <ref>PMID:11139489</ref> <ref>PMID:11741542</ref> <ref>PMID:12554866</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Baker's yeast~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Aglietti, R A~~]]	+	[[Category: Saccharomyces cerevisiae S288C]]
-	[[Category: ~~Floor, S N~~]]	+	[[Category: Aglietti RA]]
-	[[Category: ~~Gross, J D~~]]	+	[[Category: Floor SN]]
-	[[Category: ~~Hydrolase]]~~	+	[[Category: Gross JD]]
-	~~[[Category: Mrna decapping]]~~	+
-	~~[[Category: Mrna decay]]~~	+
-	~~[[Category: Nudix~~]]	+

OCA at 21:48, 4 August 2016

OCA — Thu, 04 Aug 2016 21:48:31 GMT

←Older revision		Revision as of 21:48, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain in complex with Mg (E153Q mutation)==		==Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain in complex with Mg (E153Q mutation)==
	<StructureSection load='4kg3' size='340' side='right' caption='[[4kg3]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4kg3' size='340' side='right' caption='[[4kg3]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4kg3]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KG3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4kg3]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KG3 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4k6e\|4k6e]], [[4kg4\|4kg4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4k6e\|4k6e]], [[4kg4\|4kg4]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DCP2, N1917, PSU1, YNL118C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 ~~Saccharomyces cerevisiae S288c~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DCP2, N1917, PSU1, YNL118C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=4kg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kg3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4kg3 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=4kg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kg3 OCA], [http://pdbe.org/4kg3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4kg3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kg3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4kg3" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Saccharomyces cerevisiae s288c~~]]	+	[[Category: Baker's yeast]]
	[[Category: Aglietti, R A]]		[[Category: Aglietti, R A]]
	[[Category: Floor, S N]]		[[Category: Floor, S N]]

OCA at 19:58, 24 December 2014

OCA — Wed, 24 Dec 2014 19:58:07 GMT

←Older revision		Revision as of 19:58, 24 December 2014
Line 8:		Line 8:
	<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=4kg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kg3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4kg3 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=4kg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kg3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4kg3 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DCP2_YEAST DCP2_YEAST]] Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.<ref>PMID:10508173</ref> <ref>PMID:11139489</ref> <ref>PMID:11741542</ref> <ref>PMID:12554866</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 14:46, 21 December 2014

OCA — Sun, 21 Dec 2014 14:46:06 GMT

←Older revision		Revision as of 14:46, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4kg3\| PDB=4kg3 \| SCENE= }}~~	+	==Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain in complex with Mg (E153Q mutation)==
-	===Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain in complex with Mg (E153Q mutation)===	+	<StructureSection load='4kg3' size='340' side='right' caption='[[4kg3]], [[Resolution\|resolution]] 1.70Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23911090}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4kg3]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KG3 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4k6e\|4k6e]], [[4kg4\|4kg4]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DCP2, N1917, PSU1, YNL118C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</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=4kg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kg3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4kg3 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Removal of the 5' cap structure by Dcp2 is a major step in several 5'-3' mRNA decay pathways. The activity of Dcp2 is enhanced by Dcp1 and bound coactivators, yet the details of how these interactions are linked to chemistry are poorly understood. Here, we report three crystal structures of the catalytic Nudix hydrolase domain of Dcp2 that demonstrate binding of a catalytically essential metal ion, and enzyme kinetics are used to identify several key active site residues involved in acid/base chemistry of decapping. Using nuclear magnetic resonance and molecular dynamics, we find that a conserved metal binding loop on the catalytic domain undergoes conformational changes during the catalytic cycle. These findings describe key events during the chemical step of decapping, suggest local active site conformational changes are important for activity, and provide a framework to explain stimulation of catalysis by the regulatory domain of Dcp2 and associated coactivators.

-	~~==Function==~~	+	Active Site Conformational Dynamics Are Coupled to Catalysis in the mRNA Decapping Enzyme Dcp2.,Aglietti RA, Floor SN, McClendon CL, Jacobson MP, Gross JD Structure. 2013 Jul 31. pii: S0969-2126(13)00245-1. doi:, 10.1016/j.str.2013.06.021. PMID:23911090<ref>PMID:23911090</ref>
-	~~[[http://www.uniprot.org/uniprot/DCP2_YEAST DCP2_YEAST]] Catalytic component of~~ the ~~decapping complex necessary for the degradation of mRNAs, both in normal~~ mRNA ~~turnover and in nonsense-mediated mRNA decay~~. ~~Removes the 7-methyl guanine cap structure from mRNA molecules~~, ~~yielding a 5'~~-~~phosphorylated mRNA fragment and 7m~~-~~GDP~~. ~~Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation~~, ~~decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body~~.~~<ref>PMID:10508173<~~/~~ref> <ref>~~PMID:~~11139489</ref> <ref>PMID:11741542</ref>~~ <ref>PMID:~~12554866~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4kg3]] is~~ a ~~3 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4KG3 OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:023911090</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Saccharomyces cerevisiae s288c]]		[[Category: Saccharomyces cerevisiae s288c]]
-	[[Category: Aglietti, R A.]]	+	[[Category: Aglietti, R A]]
-	[[Category: Floor, S N.]]	+	[[Category: Floor, S N]]
-	[[Category: Gross, J D.]]	+	[[Category: Gross, J D]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Mrna decapping]]		[[Category: Mrna decapping]]
	[[Category: Mrna decay]]		[[Category: Mrna decay]]
	[[Category: Nudix]]		[[Category: Nudix]]

OCA at 08:26, 21 August 2013

OCA — Wed, 21 Aug 2013 08:26:52 GMT

←Older revision		Revision as of 08:26, 21 August 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4kg3\| PDB=4kg3 \| SCENE= }}
		+	===Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain in complex with Mg (E153Q mutation)===
		+	{{ABSTRACT_PUBMED_23911090}}

-	~~The entry 4kg3~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/DCP2_YEAST DCP2_YEAST]] Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.<ref>PMID:10508173</ref> <ref>PMID:11139489</ref> <ref>PMID:11741542</ref> <ref>PMID:12554866</ref>

-	~~Authors~~: ~~Aglietti, R~~.A.~~, Floor, S~~.N.~~, Gross, J~~.D.	+	==About this Structure==
		+	[[4kg3]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KG3 OCA].

-	~~Description~~: ~~Crystal structure of~~ Saccharomyces cerevisiae ~~Dcp2~~ Nudix ~~domain in complex with Mg (E153Q mutation)~~	+	==Reference==
		+	<ref group="xtra">PMID:023911090</ref><references group="xtra"/><references/>
		+	[[Category: Saccharomyces cerevisiae s288c]]
		+	[[Category: Aglietti, R A.]]
		+	[[Category: Floor, S N.]]
		+	[[Category: Gross, J D.]]
		+	[[Category: Hydrolase]]
		+	[[Category: Mrna decapping]]
		+	[[Category: Mrna decay]]
		+	[[Category: Nudix]]

OCA at 19:58, 7 August 2013

OCA — Wed, 07 Aug 2013 19:58:33 GMT

←Older revision		Revision as of 19:58, 7 August 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4kg3 is ON HOLD	+	The entry 4kg3 is ON HOLD until Paper Publication

	Authors: Aglietti, R.A., Floor, S.N., Gross, J.D.		Authors: Aglietti, R.A., Floor, S.N., Gross, J.D.

	Description: Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain in complex with Mg (E153Q mutation)		Description: Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain in complex with Mg (E153Q mutation)

OCA: Protected "4kg3" [edit=sysop:move=sysop]

OCA — Wed, 08 May 2013 07:22:24 GMT

Protected "4kg3" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:22, 8 May 2013

OCA: New page: '''Unreleased structure''' The entry 4kg3 is ON HOLD Authors: Aglietti, R.A., Floor, S.N., Gross, J.D. Description: Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain in c...

OCA — Wed, 08 May 2013 07:22:23 GMT

New page: '''Unreleased structure''' The entry 4kg3 is ON HOLD Authors: Aglietti, R.A., Floor, S.N., Gross, J.D. Description: Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain in c...

New page

'''Unreleased structure'''

The entry 4kg3 is ON HOLD

Authors: Aglietti, R.A., Floor, S.N., Gross, J.D.

Description: Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain in complex with Mg (E153Q mutation)