6scx - Revision history

OCA at 12:39, 24 January 2024

OCA — Wed, 24 Jan 2024 12:39:33 GMT

←Older revision		Revision as of 12:39, 24 January 2024
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	<StructureSection load='6scx' size='340' side='right'caption='[[6scx]], [[Resolution\|resolution]] 2.92Å' scene=''>		<StructureSection load='6scx' size='340' side='right'caption='[[6scx]], [[Resolution\|resolution]] 2.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6scx]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6SCX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6scx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SCX FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=CD:CADMIUM+ION'>CD</scene~~>, ~~<scene name='pdbligand=MGP:7-METHYL-GUANOSINE-5-TRIPHOSPHATE'>MGP</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]] 2.92Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[http:~~/~~/en.wikipedia.org/wiki/NAD(+)_diphosphatase NAD(+) diphosphatase]~~, ~~with EC number [http~~:~~//www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=3.6.1.22 3.6.1.22]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MGP:7-METHYL-GUANOSINE-5-TRIPHOSPHATE'>MGP</scene></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=6scx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scx OCA], [~~http~~://pdbe.org/6scx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6scx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6scx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6scx 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=6scx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scx OCA], [https://pdbe.org/6scx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6scx RCSB], [https://www.ebi.ac.uk/pdbsum/6scx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6scx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/NUD12_HUMAN NUD12_HUMAN]] Hydrolyzes NAD(P)H to NMNH and AMP (2',5'-ADP), and diadenosine diphosphate to AMP. Has also activity towards NAD(P)(+), ADP-ribose and diadenosine triphosphate. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle.<ref>PMID:12790796</ref>	+	[https://www.uniprot.org/uniprot/NUD12_HUMAN NUD12_HUMAN] Hydrolyzes NAD(P)H to NMNH and AMP (2',5'-ADP), and diadenosine diphosphate to AMP. Has also activity towards NAD(P)(+), ADP-ribose and diadenosine triphosphate. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle.<ref>PMID:12790796</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: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chen~~, K M~~]]	+	[[Category: Chen KM]]
-	[[Category: Fleury-Olela, F]]	+	[[Category: Fleury-Olela F]]
-	[[Category: Gos, P]]	+	[[Category: Gos P]]
-	[[Category: Homolka, D]]	+	[[Category: Homolka D]]
-	[[Category: Li, L]]	+	[[Category: Li L]]
-	[[Category: McCarthy~~, A A~~]]	+	[[Category: McCarthy AA]]
-	[[Category: Pillai~~, R S~~]]	+	[[Category: Pillai RS]]
-	[[Category: Wu, H]]	+	[[Category: Wu H]]
-	~~[[Category: Denadding enzyme]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Nudix protein~~]]	+

OCA at 07:40, 8 January 2020

OCA — Wed, 08 Jan 2020 07:40:34 GMT

←Older revision		Revision as of 07:40, 8 January 2020
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-	'''Unreleased structure'''

-	~~The entry~~ 6scx is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal structure of the catalytic domain of human NUDT12 in complex with 7-methyl-guanosine-5'-triphosphate==
		+	<StructureSection load='6scx' size='340' side='right'caption='[[6scx]], [[Resolution\|resolution]] 2.92Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6scx]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SCX FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MGP:7-METHYL-GUANOSINE-5-TRIPHOSPHATE'>MGP</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_diphosphatase NAD(+) diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.22 3.6.1.22] </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=6scx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scx OCA], [http://pdbe.org/6scx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6scx RCSB], [http://www.ebi.ac.uk/pdbsum/6scx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6scx ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NUD12_HUMAN NUD12_HUMAN]] Hydrolyzes NAD(P)H to NMNH and AMP (2',5'-ADP), and diadenosine diphosphate to AMP. Has also activity towards NAD(P)(+), ADP-ribose and diadenosine triphosphate. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle.<ref>PMID:12790796</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	RNA polymerase II transcripts receive a protective 5',5'-triphosphate-linked 7-methylguanosine (m(7)G) cap, and its removal by decapping enzymes like DCP2 is critical for initiation of RNA decay. Alternative RNA caps can be acquired when transcription initiation uses metabolites like nicotinamide adenine dinucleotide (NAD), generating NAD-RNAs. Here, we identify human NUDT12 as a cytosolic NAD-RNA decapping enzyme. NUDT12 is active only as homodimers, with each monomer contributing to creation of the two functional catalytic pockets. We identify an approximately 600-kDa dodecamer complex between bleomycin hydrolase (BLMH) and NUDT12, with BLMH being required for localization of NUDT12 to a few discrete cytoplasmic granules that are distinct from P-bodies. Both proteins downregulate gene expression when artificially tethered to a reporter RNA in vivo. Furthermore, loss of Nudt12 results in a significant upregulation of circadian clock transcripts in mouse liver. Overall, our study points to a physiological role for NUDT12 in the cytosolic surveillance of NAD-RNAs.

-	~~Authors~~:	+	Decapping Enzyme NUDT12 Partners with BLMH for Cytoplasmic Surveillance of NAD-Capped RNAs.,Wu H, Li L, Chen KM, Homolka D, Gos P, Fleury-Olela F, McCarthy AA, Pillai RS Cell Rep. 2019 Dec 24;29(13):4422-4434.e13. doi: 10.1016/j.celrep.2019.11.108. PMID:31875550<ref>PMID:31875550</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6scx" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Chen, K M]]
		+	[[Category: Fleury-Olela, F]]
		+	[[Category: Gos, P]]
		+	[[Category: Homolka, D]]
		+	[[Category: Li, L]]
		+	[[Category: McCarthy, A A]]
		+	[[Category: Pillai, R S]]
		+	[[Category: Wu, H]]
		+	[[Category: Denadding enzyme]]
		+	[[Category: Hydrolase]]
		+	[[Category: Nudix protein]]

OCA at 03:39, 10 October 2019

OCA — Thu, 10 Oct 2019 03:39:40 GMT

←Older revision		Revision as of 03:39, 10 October 2019
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6scx is ON HOLD	+	The entry 6scx is ON HOLD until Paper Publication

	Authors:		Authors:

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

OCA — Wed, 31 Jul 2019 04:59:07 GMT

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

←Older revision

Revision as of 04:59, 31 July 2019

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

OCA — Wed, 31 Jul 2019 04:59:05 GMT

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

New page

'''Unreleased structure'''

The entry 6scx is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]