4lt6: Difference between revisions
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==Crystal Structure of human poly(A) polymerase gamma== | |||
<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 [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LT6 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3AT:3-DEOXYADENOSINE-5-TRIPHOSPHATE'>3AT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAPOLG, PAP2, PAPG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Polynucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.19 2.7.7.19] </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=4lt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lt6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lt6 RCSB], [http://www.ebi.ac.uk/pdbsum/4lt6 PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
== | ==See Also== | ||
*[[Poly(A) Polymerase|Poly(A) Polymerase]] | |||
*[[RNA polymerase|RNA polymerase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Polynucleotide adenylyltransferase]] | [[Category: Polynucleotide adenylyltransferase]] | ||
[[Category: Doublie, S | [[Category: Doublie, S]] | ||
[[Category: Keller, W | [[Category: Keller, W]] | ||
[[Category: Martin, G | [[Category: Martin, G]] | ||
[[Category: Nausch, L | [[Category: Nausch, L]] | ||
[[Category: Yang, Q | [[Category: Yang, Q]] | ||
[[Category: 3' processing]] | [[Category: 3' processing]] | ||
[[Category: Mrna processing]] | [[Category: Mrna processing]] | ||
Revision as of 20:34, 21 December 2014
Crystal Structure of human poly(A) polymerase gammaCrystal Structure of human poly(A) polymerase gamma
Structural highlights
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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