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6scx

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Current revision

Crystal structure of the catalytic domain of human NUDT12 in complex with 7-methyl-guanosine-5'-triphosphate

Structural highlights

6scx is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.92Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1]

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Abdelraheim SR, Spiller DG, McLennan AG. Mammalian NADH diphosphatases of the Nudix family: cloning and characterization of the human peroxisomal NUDT12 protein. Biochem J. 2003 Sep 1;374(Pt 2):329-35. doi: 10.1042/BJ20030441. PMID:12790796 doi:http://dx.doi.org/10.1042/BJ20030441
↑ Wu H, Li L, Chen KM, Homolka D, Gos P, Fleury-Olela F, McCarthy AA, Pillai RS. Decapping Enzyme NUDT12 Partners with BLMH for Cytoplasmic Surveillance of NAD-Capped RNAs. Cell Rep. 2019 Dec 24;29(13):4422-4434.e13. doi: 10.1016/j.celrep.2019.11.108. PMID:31875550 doi:http://dx.doi.org/10.1016/j.celrep.2019.11.108

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6scx"

@@ Line 3: / Line 3: @@
 <StructureSection load='6scx' size='340' side='right'caption='[[6scx]], [[Resolution|resolution]] 2.92&Aring;' 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>
+<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]] 2.92&#8491;</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>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[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]]

6scx

From Proteopedia

Current revision

Crystal structure of the catalytic domain of human NUDT12 in complex with 7-methyl-guanosine-5'-triphosphate

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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