View source for 5a2x


==Crystal structure of mtPAP in complex with CTP==
<StructureSection load='5a2x' size='340' side='right'caption='[[5a2x]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5a2x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A2X 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]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5a2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a2x OCA], [https://pdbe.org/5a2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a2x RCSB], [https://www.ebi.ac.uk/pdbsum/5a2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a2x ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F1NBW0_CHICK F1NBW0_CHICK] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Polyadenylation, performed by poly(A) polymerases (PAPs), is a ubiquitous post-transcriptional modification that plays key roles in multiple aspects of RNA metabolism. Although cytoplasmic and nuclear PAPs have been studied extensively, the mechanism by which mitochondrial PAP (mtPAP) selects adenosine triphosphate over other nucleotides is unknown. Furthermore, mtPAP is unique because it acts as a dimer. However, mtPAP's dimerization requirement remains enigmatic. Here, we show the structural basis for mtPAP's nucleotide selectivity, dimerization and catalysis. Our structures reveal an intricate dimerization interface that features an RNA-recognition module formed through strand complementation. Further, we propose the structural basis for the N478D mutation that drastically reduces the length of poly(A) tails on mitochondrial mRNAs in patients with spastic ataxia 4 (SPAX4), a severe and progressive neurodegenerative disease.

Structure of mitochondrial poly(A) RNA polymerase reveals the structural basis for dimerization, ATP selectivity and the SPAX4 disease phenotype.,Lapkouski M, Hallberg BM Nucleic Acids Res. 2015 Aug 28. pii: gkv861. PMID:26319014<ref>PMID:26319014</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5a2x" style="background-color:#fffaf0;"></div>

==See Also==
*[[Poly(A) polymerase 3D structures|Poly(A) polymerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Hallberg BM]]
[[Category: Lapkouski M]]