3ouy: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ouy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OUY FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ouy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OUY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <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]] 2.69&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ov7|3ov7]], [[3ova|3ova]], [[3ovb|3ovb]], [[3ovs|3ovs]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <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=3ouy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ouy OCA], [https://pdbe.org/3ouy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ouy RCSB], [https://www.ebi.ac.uk/pdbsum/3ouy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ouy ProSAT]</span></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=3ouy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ouy OCA], [https://pdbe.org/3ouy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ouy RCSB], [https://www.ebi.ac.uk/pdbsum/3ouy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ouy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CCA_ARCFU CCA_ARCFU]] Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.<ref>PMID:14592988</ref> 
[https://www.uniprot.org/uniprot/CCA_ARCFU CCA_ARCFU] Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.<ref>PMID:14592988</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CCA-adding enzymes [ATP(CTP):tRNA nucleotidyltransferases] add CCA onto the 3' end of transfer RNA (tRNA) precursors without using a nucleic acid template. Although the mechanism by which cytosine (C) is selected at position 75 of tRNA has been established, the mechanism by which adenine (A) is selected at position 76 remains elusive. Here, we report five cocrystal structures of the enzyme complexed with both a tRNA mimic and nucleoside triphosphates under catalytically active conditions. These structures suggest that adenosine 5'-monophosphate is incorporated onto the A76 position of the tRNA via a carboxylate-assisted, one-metal-ion mechanism with aspartate 110 functioning as a general base. The discrimination against incorporation of cytidine 5'-triphosphate (CTP) at position 76 arises from improper placement of the alpha phosphate of the incoming CTP, which results from the interaction of C with arginine 224 and prevents the nucleophilic attack by the 3' hydroxyl group of cytidine75.
 
How the CCA-adding enzyme selects adenine over cytosine at position 76 of tRNA.,Pan B, Xiong Y, Steitz TA Science. 2010 Nov 12;330(6006):937-40. PMID:21071662<ref>PMID:21071662</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ouy" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pan, B C]]
[[Category: Pan BC]]
[[Category: Steitz, T A]]
[[Category: Steitz TA]]
[[Category: Xiong, Y]]
[[Category: Xiong Y]]
[[Category: Cca-adding]]
[[Category: Phospholation]]
[[Category: Protein-rna complex]]
[[Category: Rossmann fold]]
[[Category: Transferase-rna complex]]
[[Category: Trna]]

Latest revision as of 13:36, 21 February 2024

How the CCA-adding Enzyme Selects Adenine Over Cytosine at Position 76 of tRNAHow the CCA-adding Enzyme Selects Adenine Over Cytosine at Position 76 of tRNA

Structural highlights

3ouy is a 4 chain structure with sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.69Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCA_ARCFU Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.[1]

See Also

References

  1. ↑ Okabe M, Tomita K, Ishitani R, Ishii R, Takeuchi N, Arisaka F, Nureki O, Yokoyama S. Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure. EMBO J. 2003 Nov 3;22(21):5918-27. PMID:14592988 doi:http://dx.doi.org/10.1093/emboj/cdg563

3ouy, resolution 2.69Å

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