3aql

<StructureSection load='3aql' size='340' side='right' caption='[[3aql]], [[Resolution|resolution]] 3.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[3aql]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecod1 Ecod1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AQL FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3aqk|3aqk]], [[3aqm|3aqm]], [[3aqn|3aqn]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EcDH1_3459 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=536056 ECOD1])</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=3aql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aql OCA], [http://pdbe.org/3aql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aql RCSB], [http://www.ebi.ac.uk/pdbsum/3aql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aql ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

PolyA polymerase (PAP) adds a polyA tail onto the 3'-end of RNAs without a nucleic acid template, using adenosine-5'-triphosphate (ATP) as a substrate. The mechanism for the substrate selection by eubacterial PAP remains obscure. Structural and biochemical studies of Escherichia coli PAP (EcPAP) revealed that the shape and size of the nucleobase-interacting pocket of EcPAP are maintained by an intra-molecular hydrogen-network, making it suitable for the accommodation of only ATP, using a single amino acid, Arg(197). The pocket structure is sustained by interactions between the catalytic domain and the RNA-binding domain. EcPAP has a flexible basic C-terminal region that contributes to optimal RNA translocation for processive adenosine 5'-monophosphate (AMP) incorporations onto the 3'-end of RNAs. A comparison of the EcPAP structure with those of other template-independent RNA polymerases suggests that structural changes of domain(s) outside the conserved catalytic core domain altered the substrate specificities of the template-independent RNA polymerases.

Mechanism for the alteration of the substrate specificities of template-independent RNA polymerases.,Toh Y, Takeshita D, Nagaike T, Numata T, Tomita K Structure. 2011 Feb 9;19(2):232-43. PMID:21300291<ref>PMID:21300291</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 3aql" style="background-color:#fffaf0;"></div>

*[[Poly(A) Polymerase|Poly(A) Polymerase]]

[[Category: Ecod1]]

[[Category: Polynucleotide adenylyltransferase]]

[[Category: Takeshita, D]]

[[Category: Toh, Y]]

[[Category: Tomita , K]]

[[Category: Transferase/rna]]