3aql: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3aql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aql OCA], [https://pdbe.org/3aql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aql RCSB], [https://www.ebi.ac.uk/pdbsum/3aql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aql ProSAT]</span></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=3aql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aql OCA], [https://pdbe.org/3aql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aql RCSB], [https://www.ebi.ac.uk/pdbsum/3aql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aql ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== 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>


==See Also==
==See Also==
*[[Poly(A) polymerase 3D structures|Poly(A) polymerase 3D structures]]
*[[Poly(A) polymerase 3D structures|Poly(A) polymerase 3D structures]]
== References ==
<references/>
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__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 14:01, 13 March 2024

Structure of bacterial protein (apo form II)

3aql, resolution 3.00Å

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