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4wc2

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Crystal structure of tRNA nucleotidyltransferase complexed with a primer tRNA and an incoming ATP analog

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Retrieved from "http://52.214.119.220/wiki/index.php/4wc2"

Categories: Aquifex aeolicus VF5 | Large Structures | Thermotoga maritima MSB8 | Tomita K | Yamashita S

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 ==Crystal structure of tRNA nucleotidyltransferase complexed with a primer tRNA and an incoming ATP analog==
-<StructureSection load='4wc2' size='340' side='right' caption='[[4wc2]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='4wc2' size='340' side='right'caption='[[4wc2]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4wc2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WC2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WC2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4wc2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5] and [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WC2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</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]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vfg|1vfg]], [[4wby|4wby]], [[4wbz|4wbz]], [[4wc0|4wc0]], [[4wc1|4wc1]], [[4wc3|4wc3]], [[4wc4|4wc4]], [[4wc5|4wc5]], [[4wc6|4wc6]], [[4wc7|4wc7]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</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">pcnB1, aq_411 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</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=4wc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wc2 OCA], [https://pdbe.org/4wc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wc2 RCSB], [https://www.ebi.ac.uk/pdbsum/4wc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wc2 ProSAT]</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=4wc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wc2 OCA], [http://pdbe.org/4wc2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wc2 RCSB], [http://www.ebi.ac.uk/pdbsum/4wc2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wc2 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/AATNT_AQUAE AATNT_AQUAE] tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the terminal adenosine residue to tRNA (PubMed:11701927, PubMed:25914059). Can incorporate CMP into tRNA ending with C74C75 (tRNACC), with very weak efficiency (PubMed:25914059).<ref>PMID:11701927</ref> <ref>PMID:25914059</ref>
-The 3'-terminal CCA (C74C75A76-3') of tRNA is required for protein synthesis. In Aquifex aeolicus, the CCA-3' is synthesized by CC-adding and A-adding enzymes, although in most organisms, CCA is synthesized by a single CCA-adding enzyme. The mechanisms by which the A-adding enzyme adds only A76, but not C74C75, onto tRNA remained elusive. The complex structures of the enzyme with various tRNAs revealed the presence of a single tRNA binding site on the enzyme, with the enzyme measuring the acceptor-TPsiC helix length of tRNA. The 3'-C75 of tRNA lacking A76 can reach the active site and the size and shape of the nucleotide binding pocket at the insertion stage are suitable for ATP. The 3'-C74 of tRNA lacking C75A76 cannot reach the active site, although CTP or ATP can bind the active pocket. Thus, the A-adding enzyme adds only A76, but not C74C75, onto tRNA.
-Measurement of Acceptor-TPsiC Helix Length of tRNA for Terminal A76-Addition by A-Adding Enzyme.,Yamashita S, Martinez A, Tomita K Structure. 2015 May 5;23(5):830-42. doi: 10.1016/j.str.2015.03.013. Epub 2015 Apr, 23. PMID:25914059<ref>PMID:25914059</ref>
+==See Also==
+*[[Poly(A) polymerase 3D structures|Poly(A) polymerase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4wc2" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Aquae]]
+[[Category: Aquifex aeolicus VF5]]
-[[Category: Tomita, K]]
+[[Category: Large Structures]]
-[[Category: Yamashita, S]]
+[[Category: Thermotoga maritima MSB8]]
-[[Category: A-adding enzyme]]
+[[Category: Tomita K]]
-[[Category: Cca-adding enzyme]]
+[[Category: Yamashita S]]
-[[Category: Rna nucleotidyltransferase]]
-[[Category: Transferase-rna complex]]

4wc2

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Crystal structure of tRNA nucleotidyltransferase complexed with a primer tRNA and an incoming ATP analog

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