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| | ==tRNA processing enzyme (apo form 1)== | | ==tRNA processing enzyme (apo form 1)== |
| - | <StructureSection load='3wfo' size='340' side='right' caption='[[3wfo]], [[Resolution|resolution]] 3.40Å' scene=''> | + | <StructureSection load='3wfo' size='340' side='right'caption='[[3wfo]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wfo]] is a 3 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=3WFO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WFO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wfo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WFO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wfp|3wfp]], [[3wfq|3wfq]], [[3wfr|3wfr]], [[3wfs|3wfs]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcnB2 ([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=3wfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wfo OCA], [https://pdbe.org/3wfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wfo RCSB], [https://www.ebi.ac.uk/pdbsum/3wfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wfo 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/CCA_tRNA_nucleotidyltransferase CCA tRNA nucleotidyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.72 2.7.7.72] </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=3wfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wfo OCA], [http://pdbe.org/3wfo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wfo RCSB], [http://www.ebi.ac.uk/pdbsum/3wfo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wfo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/CATNT_AQUAE CATNT_AQUAE] tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the two cytidine residues to tRNA.<ref>PMID:11701927</ref> <ref>PMID:24389024</ref> |
| - | The 3'-terminal CCA (CCA-3' at positions 74-76) of tRNA is synthesized by CCA-adding enzyme using CTP and ATP as substrates, without a nucleic acid template. In Aquifex aeolicus, CC-adding and A-adding enzymes collaboratively synthesize the CCA-3'. The mechanism of CCA-3' synthesis by these two enzymes remained obscure. We now present crystal structures representing CC addition onto tRNA by A. aeolicus CC-adding enzyme. After C(7)(4) addition in an enclosed active pocket and pyrophosphate release, the tRNA translocates and rotates relative to the enzyme, and C(7)(5) addition occurs in the same active pocket as C(7)(4) addition. At both the C(7)(4)-adding and C(7)(5)-adding stages, CTP is selected by Watson-Crick-like hydrogen bonds between the cytosine of CTP and conserved Asp and Arg residues in the pocket. After C(7)(4)C(7)(5) addition and pyrophosphate release, the tRNA translocates further and drops off the enzyme, and the CC-adding enzyme terminates RNA polymerization.
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| - | Translocation and rotation of tRNA during template-independent RNA polymerization by tRNA nucleotidyltransferase.,Yamashita S, Takeshita D, Tomita K Structure. 2014 Feb 4;22(2):315-25. doi: 10.1016/j.str.2013.12.002. Epub 2014 Jan, 2. PMID:24389024<ref>PMID:24389024</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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| - | <div class="pdbe-citations 3wfo" style="background-color:#fffaf0;"></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 == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aquae]] | + | [[Category: Aquifex aeolicus VF5]] |
| - | [[Category: CCA tRNA nucleotidyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Takeshita, D]] | + | [[Category: Takeshita D]] |
| - | [[Category: Tomita, K]] | + | [[Category: Tomita K]] |
| - | [[Category: Yamashita, S]] | + | [[Category: Yamashita S]] |
| - | [[Category: Terminal nucleotide transferase]]
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| - | [[Category: Transferase]]
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