View source for 3wfp


==tRNA processing enzyme (apo form 2)==
<StructureSection load='3wfp' size='340' side='right'caption='[[3wfp]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wfp]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WFP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.005&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wfp OCA], [https://pdbe.org/3wfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wfp RCSB], [https://www.ebi.ac.uk/pdbsum/3wfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wfp ProSAT]</span></td></tr>
</table>
== Function ==
[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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wfp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Poly(A) polymerase 3D structures|Poly(A) polymerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquifex aeolicus VF5]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Takeshita D]]
[[Category: Tomita K]]
[[Category: Yamashita S]]