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5wu3

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Revision as of 07:17, 7 October 2020

Crystal structure of human Tut1 bound with MgUTP, form II

Structural highlights

5wu3 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	5wu6, 5wu5, 5wu4, 5wu2, 5wu1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[STPAP_HUMAN] Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation.^[1] ^[2] ^[3]

Publication Abstract from PubMed

The terminal uridylyltransferase, TUT1, builds or repairs the 3'-oligo-uridylylated tail of U6 snRNA. The 3'-oligo-uridylylated tail is the Lsm-binding site for U4/U6 di-snRNP formation and U6 snRNA recycling for pre-mRNA splicing. Here, we report crystallographic and biochemical analyses of human TUT1, which revealed the mechanisms for the specific uridylylation of the 3'-end of U6 snRNA by TUT1. The O2 and O4 atoms of the UTP base form hydrogen bonds with the conserved His and Asn in the catalytic pocket, respectively, and TUT1 preferentially incorporates UMP onto the 3'-end of RNAs. TUT1 recognizes the entire U6 snRNA molecule by its catalytic domains, N-terminal RNA-recognition motifs and a previously unidentified C-terminal RNA-binding domain. Each domain recognizes specific regions within U6 snRNA, and the recognition is coupled with the domain movements and U6 snRNA structural changes. Hence, TUT1 functions as the U6 snRNA-specific terminal uridylyltransferase required for pre-mRNA splicing.

Crystal structures of U6 snRNA-specific terminal uridylyltransferase.,Yamashita S, Takagi Y, Nagaike T, Tomita K Nat Commun. 2017 Jun 7;8:15788. doi: 10.1038/ncomms15788. PMID:28589955^[4]

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

References

↑ Trippe R, Guschina E, Hossbach M, Urlaub H, Luhrmann R, Benecke BJ. Identification, cloning, and functional analysis of the human U6 snRNA-specific terminal uridylyl transferase. RNA. 2006 Aug;12(8):1494-504. Epub 2006 Jun 21. PMID:16790842 doi:http://dx.doi.org/rna.87706
↑ Mellman DL, Gonzales ML, Song C, Barlow CA, Wang P, Kendziorski C, Anderson RA. A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs. Nature. 2008 Feb 21;451(7181):1013-7. doi: 10.1038/nature06666. PMID:18288197 doi:http://dx.doi.org/10.1038/nature06666
↑ Laishram RS, Anderson RA. The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA. EMBO J. 2010 Dec 15;29(24):4132-45. doi: 10.1038/emboj.2010.287. Epub 2010 Nov, 19. PMID:21102410 doi:http://dx.doi.org/10.1038/emboj.2010.287
↑ Yamashita S, Takagi Y, Nagaike T, Tomita K. Crystal structures of U6 snRNA-specific terminal uridylyltransferase. Nat Commun. 2017 Jun 7;8:15788. doi: 10.1038/ncomms15788. PMID:28589955 doi:http://dx.doi.org/10.1038/ncomms15788

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5wu3"

Categories: Large Structures | Tomita, K | Yamashita, S | Terminal nucleotidyl transferase | Transferase

@@ Line 1: / Line 1: @@
 ==Crystal structure of human Tut1 bound with MgUTP, form II==
-<StructureSection load='5wu3' size='340' side='right' caption='[[5wu3]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='5wu3' size='340' side='right'caption='[[5wu3]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5wu3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WU3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5wu3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WU3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WU3 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wu6|5wu6]], [[5wu5|5wu5]], [[5wu4|5wu4]], [[5wu2|5wu2]], [[5wu1|5wu1]]</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=5wu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wu3 OCA], [http://pdbe.org/5wu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wu3 RCSB], [http://www.ebi.ac.uk/pdbsum/5wu3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wu3 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=5wu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wu3 OCA], [http://pdbe.org/5wu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wu3 RCSB], [http://www.ebi.ac.uk/pdbsum/5wu3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wu3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5wu3" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Poly(A) Polymerase|Poly(A) Polymerase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Tomita, K]]
 [[Category: Yamashita, S]]
 [[Category: Terminal nucleotidyl transferase]]
 [[Category: Transferase]]

5wu3

From Proteopedia

Revision as of 07:17, 7 October 2020

Crystal structure of human Tut1 bound with MgUTP, form II

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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