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| ==Structure of bacterial protein (apo form II)== | | ==Structure of bacterial protein (apo form II)== |
| <StructureSection load='3aql' size='340' side='right' caption='[[3aql]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='3aql' size='340' side='right'caption='[[3aql]], [[Resolution|resolution]] 3.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3aql]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_dh1 Escherichia coli dh1]. 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> | | <table><tr><td colspan='2'>[[3aql]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_DH1 Escherichia coli DH1]. 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 [https://proteopedia.org/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> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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 Escherichia coli DH1])</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> |
| <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>
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| <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://www.rcsb.org/pdb/explore.do?structureId=3aql RCSB], [http://www.ebi.ac.uk/pdbsum/3aql PDBsum]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| ==See Also== | | ==See Also== |
| *[[Poly(A) Polymerase|Poly(A) Polymerase]] | | *[[Poly(A) polymerase 3D structures|Poly(A) polymerase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Escherichia coli dh1]] | | [[Category: Escherichia coli DH1]] |
| [[Category: Polynucleotide adenylyltransferase]] | | [[Category: Large Structures]] |
| [[Category: Takeshita, D]] | | [[Category: Takeshita D]] |
| [[Category: Toh, Y]] | | [[Category: Toh Y]] |
| [[Category: Tomita , K]] | | [[Category: Tomita K]] |
| [[Category: A-phosphorylation]]
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| [[Category: Atp binding]]
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| [[Category: Atp-binding]]
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| [[Category: Nucleotide-binding]]
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| [[Category: Nucleotidyltransferase]]
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| [[Category: Rna-binding]]
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| [[Category: Transferase]]
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| [[Category: Transferase/rna]]
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