6trq - Revision history

OCA at 14:33, 6 March 2024

2024-03-06T14:33:33Z

←Older revision		Revision as of 14:33, 6 March 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DCPS_YEAST DCPS_YEAST] Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP) or tri-methyl guanosine nucleoside monophosphate (m3(2,2,7)GMP), respectively. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to (m(7)GMP) and m3(2,2,7)GMP, respectively (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCS1 to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. May also regulates the 5'->3' exoribonucleolytic mRNA decay pathway in a cap-independent manner. Negatively regulates trehalase activity.<ref>PMID:12198172</ref> <ref>PMID:14523240</ref> <ref>PMID:15240832</ref> <ref>PMID:15273322</ref> <ref>PMID:16260594</ref> <ref>PMID:16963086</ref> <ref>PMID:22985415</ref>		[https://www.uniprot.org/uniprot/DCPS_YEAST DCPS_YEAST] Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP) or tri-methyl guanosine nucleoside monophosphate (m3(2,2,7)GMP), respectively. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to (m(7)GMP) and m3(2,2,7)GMP, respectively (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCS1 to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. May also regulates the 5'->3' exoribonucleolytic mRNA decay pathway in a cap-independent manner. Negatively regulates trehalase activity.<ref>PMID:12198172</ref> <ref>PMID:14523240</ref> <ref>PMID:15240832</ref> <ref>PMID:15273322</ref> <ref>PMID:16260594</ref> <ref>PMID:16963086</ref> <ref>PMID:22985415</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The 5' messenger RNA (mRNA) cap structure enhances translation and protects the transcript against exonucleolytic degradation. During mRNA turnover, this cap is removed from the mRNA. This decapping step is catalyzed by the Scavenger Decapping Enzyme (DcpS), in case the mRNA has been exonucleolyticly shortened from the 3' end by the exosome complex. Here, we show that DcpS only processes mRNA fragments that are shorter than three nucleotides in length. Based on a combination of methyl transverse relaxation optimized (TROSY) NMR spectroscopy and X-ray crystallography, we established that the DcpS substrate length-sensing mechanism is based on steric clashes between the enzyme and the third nucleotide of a capped mRNA. For longer mRNA substrates, these clashes prevent conformational changes in DcpS that are required for the formation of a catalytically competent active site. Point mutations that enlarge the space for the third nucleotide in the mRNA body enhance the activity of DcpS on longer mRNA species. We find that this mechanism to ensure that the enzyme is not active on translating long mRNAs is conserved from yeast to humans. Finally, we show that the products that the exosome releases after 3' to 5' degradation of the mRNA body are indeed short enough to be decapped by DcpS. Our data thus directly confirms the notion that mRNA products of the exosome are direct substrates for DcpS. In summary, we demonstrate a direct relationship between conformational changes and enzyme activity that is exploited to achieve substrate selectivity.
-
-	Molecular basis of the selective processing of short mRNA substrates by the DcpS mRNA decapping enzyme.,Fuchs AL, Wurm JP, Neu A, Sprangers R Proc Natl Acad Sci U S A. 2020 Jul 28. pii: 2009362117. doi:, 10.1073/pnas.2009362117. PMID:32723815<ref>PMID:32723815</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 6trq" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:07, 24 January 2024

2024-01-24T13:07:58Z

←Older revision		Revision as of 13:07, 24 January 2024
Line 3:		Line 3:
	<StructureSection load='6trq' size='340' side='right'caption='[[6trq]], [[Resolution\|resolution]] 2.94Å' scene=''>		<StructureSection load='6trq' size='340' side='right'caption='[[6trq]], [[Resolution\|resolution]] 2.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6trq]] is a 4 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=6TRQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6TRQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6trq]] is a 4 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=6TRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TRQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0G:L-GUANOSINE-5-MONOPHOSPHATE'>0G</scene>, <scene name='pdbligand=2PO:PHOSPHONATE'>2PO</scene>, <scene name='pdbligand=M7G:7N-METHYL-8-HYDROGUANOSINE-5-DIPHOSPHATE'>M7G</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.944Å</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DCS1, YLR270W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0G:L-GUANOSINE-5-MONOPHOSPHATE'>0G</scene>, <scene name='pdbligand=2PO:PHOSPHONATE'>2PO</scene>, <scene name='pdbligand=M7G:7N-METHYL-8-HYDROGUANOSINE-5-DIPHOSPHATE'>M7G</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5'-(N(7)-methyl_5'-triphosphoguanosine)-(mRNA)_diphosphatase 5'-(N(7)-methyl 5'-triphosphoguanosine)-(mRNA) diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.59 3.6.1.59] </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=6trq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6trq OCA], [https://pdbe.org/6trq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6trq RCSB], [https://www.ebi.ac.uk/pdbsum/6trq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6trq ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6trq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6trq OCA], [~~http~~://pdbe.org/6trq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6trq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6trq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6trq ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DCPS_YEAST DCPS_YEAST]] Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP) or tri-methyl guanosine nucleoside monophosphate (m3(2,2,7)GMP), respectively. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to (m(7)GMP) and m3(2,2,7)GMP, respectively (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCS1 to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. May also regulates the 5'->3' exoribonucleolytic mRNA decay pathway in a cap-independent manner. Negatively regulates trehalase activity.<ref>PMID:12198172</ref> <ref>PMID:14523240</ref> <ref>PMID:15240832</ref> <ref>PMID:15273322</ref> <ref>PMID:16260594</ref> <ref>PMID:16963086</ref> <ref>PMID:22985415</ref>	+	[https://www.uniprot.org/uniprot/DCPS_YEAST DCPS_YEAST] Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP) or tri-methyl guanosine nucleoside monophosphate (m3(2,2,7)GMP), respectively. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to (m(7)GMP) and m3(2,2,7)GMP, respectively (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCS1 to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. May also regulates the 5'->3' exoribonucleolytic mRNA decay pathway in a cap-independent manner. Negatively regulates trehalase activity.<ref>PMID:12198172</ref> <ref>PMID:14523240</ref> <ref>PMID:15240832</ref> <ref>PMID:15273322</ref> <ref>PMID:16260594</ref> <ref>PMID:16963086</ref> <ref>PMID:22985415</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Baker's yeast]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Fuchs, A L~~]]	+	[[Category: Saccharomyces cerevisiae S288C]]
-	[[Category: ~~Neu,~~ A]]	+	[[Category: Fuchs A-L]]
-	[[Category: ~~Sprangers, R~~]]	+	[[Category: Neu A]]
-	[[Category: ~~Decapping]]~~	+	[[Category: Sprangers R]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Mrna decapping]]~~	+
-	~~[[Category: Mrna degradation~~]]	+

OCA at 10:01, 12 August 2020

2020-08-12T10:01:35Z

←Older revision		Revision as of 10:01, 12 August 2020
Line 1:		Line 1:

	==S.c. Scavenger Decapping Enzyme DcpS in complex with the capped RNA dinucleotide m7G-GU==		==S.c. Scavenger Decapping Enzyme DcpS in complex with the capped RNA dinucleotide m7G-GU==
-	<StructureSection load='6trq' size='340' side='right'caption='[[6trq]]' scene=''>	+	<StructureSection load='6trq' size='340' side='right'caption='[[6trq]], [[Resolution\|resolution]] 2.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TRQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TRQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6trq]] is a 4 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=6TRQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TRQ FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6trq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6trq OCA], [http://pdbe.org/6trq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6trq RCSB], [http://www.ebi.ac.uk/pdbsum/6trq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6trq ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0G:L-GUANOSINE-5-MONOPHOSPHATE'>0G</scene>, <scene name='pdbligand=2PO:PHOSPHONATE'>2PO</scene>, <scene name='pdbligand=M7G:7N-METHYL-8-HYDROGUANOSINE-5-DIPHOSPHATE'>M7G</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DCS1, YLR270W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5'-(N(7)-methyl_5'-triphosphoguanosine)-(mRNA)_diphosphatase 5'-(N(7)-methyl 5'-triphosphoguanosine)-(mRNA) diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.59 3.6.1.59] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6trq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6trq OCA], [http://pdbe.org/6trq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6trq RCSB], [http://www.ebi.ac.uk/pdbsum/6trq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6trq ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DCPS_YEAST DCPS_YEAST]] Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP) or tri-methyl guanosine nucleoside monophosphate (m3(2,2,7)GMP), respectively. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to (m(7)GMP) and m3(2,2,7)GMP, respectively (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCS1 to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. May also regulates the 5'->3' exoribonucleolytic mRNA decay pathway in a cap-independent manner. Negatively regulates trehalase activity.<ref>PMID:12198172</ref> <ref>PMID:14523240</ref> <ref>PMID:15240832</ref> <ref>PMID:15273322</ref> <ref>PMID:16260594</ref> <ref>PMID:16963086</ref> <ref>PMID:22985415</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The 5' messenger RNA (mRNA) cap structure enhances translation and protects the transcript against exonucleolytic degradation. During mRNA turnover, this cap is removed from the mRNA. This decapping step is catalyzed by the Scavenger Decapping Enzyme (DcpS), in case the mRNA has been exonucleolyticly shortened from the 3' end by the exosome complex. Here, we show that DcpS only processes mRNA fragments that are shorter than three nucleotides in length. Based on a combination of methyl transverse relaxation optimized (TROSY) NMR spectroscopy and X-ray crystallography, we established that the DcpS substrate length-sensing mechanism is based on steric clashes between the enzyme and the third nucleotide of a capped mRNA. For longer mRNA substrates, these clashes prevent conformational changes in DcpS that are required for the formation of a catalytically competent active site. Point mutations that enlarge the space for the third nucleotide in the mRNA body enhance the activity of DcpS on longer mRNA species. We find that this mechanism to ensure that the enzyme is not active on translating long mRNAs is conserved from yeast to humans. Finally, we show that the products that the exosome releases after 3' to 5' degradation of the mRNA body are indeed short enough to be decapped by DcpS. Our data thus directly confirms the notion that mRNA products of the exosome are direct substrates for DcpS. In summary, we demonstrate a direct relationship between conformational changes and enzyme activity that is exploited to achieve substrate selectivity.
		+
		+	Molecular basis of the selective processing of short mRNA substrates by the DcpS mRNA decapping enzyme.,Fuchs AL, Wurm JP, Neu A, Sprangers R Proc Natl Acad Sci U S A. 2020 Jul 28. pii: 2009362117. doi:, 10.1073/pnas.2009362117. PMID:32723815<ref>PMID:32723815</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6trq" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Baker's yeast]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Fuchs A-L]]	+	[[Category: Fuchs, A L]]
-	[[Category: Neu A]]	+	[[Category: Neu, A]]
-	[[Category: Sprangers R]]	+	[[Category: Sprangers, R]]
		+	[[Category: Decapping]]
		+	[[Category: Hydrolase]]
		+	[[Category: Mrna decapping]]
		+	[[Category: Mrna degradation]]

OCA at 10:50, 22 July 2020

2020-07-22T10:50:53Z

←Older revision		Revision as of 10:50, 22 July 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6trq is ~~ON HOLD~~	+	==S.c. Scavenger Decapping Enzyme DcpS in complex with the capped RNA dinucleotide m7G-GU==
-		+	<StructureSection load='6trq' size='340' side='right'caption='[[6trq]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TRQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TRQ FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6trq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6trq OCA], [http://pdbe.org/6trq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6trq RCSB], [http://www.ebi.ac.uk/pdbsum/6trq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6trq ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Fuchs A-L]]
		+	[[Category: Neu A]]
		+	[[Category: Sprangers R]]

OCA at 13:52, 22 January 2020

2020-01-22T13:52:47Z

←Older revision		Revision as of 13:52, 22 January 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6trq is ON HOLD ~~until sometime in the future~~	+	The entry 6trq is ON HOLD

	Authors:		Authors:

OCA at 06:43, 1 January 2020

2020-01-01T06:43:16Z

←Older revision		Revision as of 06:43, 1 January 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6trq is ON HOLD	+	The entry 6trq is ON HOLD until sometime in the future

	Authors:		Authors:

OCA: Protected "6trq" [edit=sysop:move=sysop]

2019-12-25T07:26:44Z

Protected "6trq" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:26, 25 December 2019

OCA: New page: '''Unreleased structure''' The entry 6trq is ON HOLD Authors: Description: Category: Unreleased Structures

2019-12-25T07:26:42Z

New page: '''Unreleased structure''' The entry 6trq is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6trq is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]