3ouy: Difference between revisions

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{{STRUCTURE_3ouy|  PDB=3ouy  |  SCENE=  }}
==How the CCA-adding Enzyme Selects Adenine Over Cytosine at Position 76 of tRNA==
===How the CCA-adding Enzyme Selects Adenine Over Cytosine at Position 76 of tRNA===
<StructureSection load='3ouy' size='340' side='right' caption='[[3ouy]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
{{ABSTRACT_PUBMED_21071662}}
== Structural highlights ==
<table><tr><td colspan='2'>[[3ouy]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OUY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ov7|3ov7]], [[3ova|3ova]], [[3ovb|3ovb]], [[3ovs|3ovs]]</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=3ouy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ouy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ouy RCSB], [http://www.ebi.ac.uk/pdbsum/3ouy PDBsum]</span></td></tr>
</table>
<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.


==Function==
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>
[[http://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>


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[3ouy]] is a 4 chain structure with sequence from [http://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].
</div>


==Reference==
==See Also==
<ref group="xtra">PMID:021071662</ref><references group="xtra"/><references/>
*[[CCA-adding enzyme|CCA-adding enzyme]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Pan, B C.]]
[[Category: Pan, B C]]
[[Category: Steitz, T A.]]
[[Category: Steitz, T A]]
[[Category: Xiong, Y.]]
[[Category: Xiong, Y]]
[[Category: Cca-adding]]
[[Category: Cca-adding]]
[[Category: Phospholation]]
[[Category: Phospholation]]

Revision as of 10:22, 19 December 2014

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.
Ligands:, ,
Resources:FirstGlance, OCA, RCSB, PDBsum

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Pan B, Xiong Y, Steitz TA. How the CCA-adding enzyme selects adenine over cytosine at position 76 of tRNA. Science. 2010 Nov 12;330(6006):937-40. PMID:21071662 doi:10.1126/science.1194985

3ouy, resolution 2.69Å

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