|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='3wfq' size='340' side='right'caption='[[3wfq]], [[Resolution|resolution]] 3.62Å' scene=''> | | <StructureSection load='3wfq' size='340' side='right'caption='[[3wfq]], [[Resolution|resolution]] 3.62Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wfq]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WFQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WFQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wfq]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5], [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8] 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=3WFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WFQ FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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]] 3.619Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wfo|3wfo]], [[3wfp|3wfp]], [[3wfr|3wfr]], [[3wfs|3wfs]]</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=3wfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wfq OCA], [https://pdbe.org/3wfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wfq RCSB], [https://www.ebi.ac.uk/pdbsum/3wfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wfq 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>
| + | |
| - | <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=3wfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wfq OCA], [http://pdbe.org/3wfq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wfq RCSB], [http://www.ebi.ac.uk/pdbsum/3wfq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wfq ProSAT]</span></td></tr> | + | |
| | </table> | | </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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 20: |
Line 20: |
| | | | |
| | ==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: CCA tRNA nucleotidyltransferase]] | + | [[Category: Aquifex aeolicus VF5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Takeshita, D]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Tomita, K]] | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: Yamashita, S]] | + | [[Category: Takeshita D]] |
| - | [[Category: Terminal nucleotide transferase]] | + | [[Category: Tomita K]] |
| - | [[Category: Transferase-rna complex]] | + | [[Category: Yamashita S]] |
| Structural highlights
Function
CATNT_AQUAE tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the two cytidine residues to tRNA.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tomita K, Weiner AM. Collaboration between CC 3'-terminal CCA of tRNA in Aquifex aeolicus. Science. 2001 Nov 9;294(5545):1334-6. PMID:11701927 doi:10.1126/science.1063816
- ↑ Yamashita S, Takeshita D, Tomita K. Translocation and rotation of tRNA during template-independent RNA polymerization by tRNA nucleotidyltransferase. Structure. 2014 Feb 4;22(2):315-25. doi: 10.1016/j.str.2013.12.002. Epub 2014 Jan, 2. PMID:24389024 doi:http://dx.doi.org/10.1016/j.str.2013.12.002
- ↑ Yamashita S, Takeshita D, Tomita K. Translocation and rotation of tRNA during template-independent RNA polymerization by tRNA nucleotidyltransferase. Structure. 2014 Feb 4;22(2):315-25. doi: 10.1016/j.str.2013.12.002. Epub 2014 Jan, 2. PMID:24389024 doi:http://dx.doi.org/10.1016/j.str.2013.12.002
|
