4lt6: Difference between revisions
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== | ==Crystal Structure of human poly(A) polymerase gamma== | ||
[[http://www.uniprot.org/uniprot/PAPOG_HUMAN PAPOG_HUMAN | <StructureSection load='4lt6' size='340' side='right'caption='[[4lt6]], [[Resolution|resolution]] 2.79Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4lt6]] is a 2 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=4LT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LT6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.79Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3AT:3-DEOXYADENOSINE-5-TRIPHOSPHATE'>3AT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=4lt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lt6 OCA], [https://pdbe.org/4lt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lt6 RCSB], [https://www.ebi.ac.uk/pdbsum/4lt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lt6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PAPOG_HUMAN PAPOG_HUMAN] Responsible for the post-transcriptional adenylation of the 3'-terminal of mRNA precursors and several small RNAs including signal recognition particle (SRP) RNA, nuclear 7SK RNA, U2 small nuclear RNA, and ribosomal 5S RNA. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In eukaryotes, the poly(A) tail added at the 3' end of an mRNA precursor is essential for the regulation of mRNA stability and the initiation of translation. Poly(A) polymerase (PAP) is the enzyme that catalyzes the poly(A) addition reaction. Multiple isoforms of PAP have been identified in vertebrates, which originate from gene duplication, alternative splicing or post-translational modifications. The complexity of PAP isoforms suggests that they might play different roles in the cell. Phylogenetic studies indicate that vertebrate PAPs are grouped into three clades termed alpha, beta and gamma, which originated from two gene duplication events. To date, all the available PAP structures are from the PAPalpha clade. Here, we present the crystal structure of the first representative of the PAPgamma clade, human PAPgamma bound to cordycepin triphosphate (3'dATP) and Ca2+. The structure revealed that PAPgamma closely resembles its PAPalpha ortholog. An analysis of residue conservation reveals a conserved catalytic binding pocket, whereas residues at the surface of the polymerase are more divergent. | |||
Crystal Structure of Human Poly(A) Polymerase Gamma Reveals a Conserved Catalytic Core for Canonical Poly(A) Polymerases.,Yang Q, Nausch L, Martin G, Keller W, Doublie S J Mol Biol. 2013 Sep 25. pii: S0022-2836(13)00609-8. doi:, 10.1016/j.jmb.2013.09.025. PMID:24076191<ref>PMID:24076191</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4lt6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Poly(A) polymerase 3D structures|Poly(A) polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Doublie | [[Category: Doublie S]] | ||
[[Category: Keller | [[Category: Keller W]] | ||
[[Category: Martin | [[Category: Martin G]] | ||
[[Category: Nausch | [[Category: Nausch L]] | ||
[[Category: Yang | [[Category: Yang Q]] | ||
Latest revision as of 19:25, 20 September 2023
Crystal Structure of human poly(A) polymerase gammaCrystal Structure of human poly(A) polymerase gamma
Structural highlights
FunctionPAPOG_HUMAN Responsible for the post-transcriptional adenylation of the 3'-terminal of mRNA precursors and several small RNAs including signal recognition particle (SRP) RNA, nuclear 7SK RNA, U2 small nuclear RNA, and ribosomal 5S RNA. Publication Abstract from PubMedIn eukaryotes, the poly(A) tail added at the 3' end of an mRNA precursor is essential for the regulation of mRNA stability and the initiation of translation. Poly(A) polymerase (PAP) is the enzyme that catalyzes the poly(A) addition reaction. Multiple isoforms of PAP have been identified in vertebrates, which originate from gene duplication, alternative splicing or post-translational modifications. The complexity of PAP isoforms suggests that they might play different roles in the cell. Phylogenetic studies indicate that vertebrate PAPs are grouped into three clades termed alpha, beta and gamma, which originated from two gene duplication events. To date, all the available PAP structures are from the PAPalpha clade. Here, we present the crystal structure of the first representative of the PAPgamma clade, human PAPgamma bound to cordycepin triphosphate (3'dATP) and Ca2+. The structure revealed that PAPgamma closely resembles its PAPalpha ortholog. An analysis of residue conservation reveals a conserved catalytic binding pocket, whereas residues at the surface of the polymerase are more divergent. Crystal Structure of Human Poly(A) Polymerase Gamma Reveals a Conserved Catalytic Core for Canonical Poly(A) Polymerases.,Yang Q, Nausch L, Martin G, Keller W, Doublie S J Mol Biol. 2013 Sep 25. pii: S0022-2836(13)00609-8. doi:, 10.1016/j.jmb.2013.09.025. PMID:24076191[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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