3aql: Difference between revisions
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==Structure of bacterial protein (apo form II)== | |||
=== | <StructureSection load='3aql' size='340' side='right' caption='[[3aql]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== 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> | |||
</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 Escherichia coli DH1])</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://www.rcsb.org/pdb/explore.do?structureId=3aql RCSB], [http://www.ebi.ac.uk/pdbsum/3aql PDBsum]</span></td></tr> | |||
</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Poly(A) Polymerase|Poly(A) Polymerase]] | *[[Poly(A) Polymerase|Poly(A) Polymerase]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli dh1]] | [[Category: Escherichia coli dh1]] | ||
[[Category: Polynucleotide adenylyltransferase]] | [[Category: Polynucleotide adenylyltransferase]] | ||
[[Category: Takeshita, D | [[Category: Takeshita, D]] | ||
[[Category: Toh, Y | [[Category: Toh, Y]] | ||
[[Category: Tomita , K | [[Category: Tomita , K]] | ||
[[Category: A-phosphorylation]] | [[Category: A-phosphorylation]] | ||
[[Category: Atp binding]] | [[Category: Atp binding]] | ||
Revision as of 13:39, 18 December 2014
Structure of bacterial protein (apo form II)
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