4x0a: Difference between revisions

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<StructureSection load='4x0a' size='340' side='right'caption='[[4x0a]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='4x0a' size='340' side='right'caption='[[4x0a]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4x0a]] is a 2 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=4X0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X0A FirstGlance]. <br>
<table><tr><td colspan='2'>[[4x0a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5] and [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X0A FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x0b|4x0b]]</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]] 3.505&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcnB1, aq_411 ([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=4x0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x0a OCA], [https://pdbe.org/4x0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x0a RCSB], [https://www.ebi.ac.uk/pdbsum/4x0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x0a ProSAT]</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=4x0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x0a OCA], [http://pdbe.org/4x0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x0a RCSB], [http://www.ebi.ac.uk/pdbsum/4x0a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x0a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AATNT_AQUAE AATNT_AQUAE] tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the terminal adenosine residue to tRNA (PubMed:11701927, PubMed:25914059). Can incorporate CMP into tRNA ending with C74C75 (tRNACC), with very weak efficiency (PubMed:25914059).<ref>PMID:11701927</ref> <ref>PMID:25914059</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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: Large Structures]]
[[Category: Large Structures]]
[[Category: Tomita, K]]
[[Category: Thermotoga maritima MSB8]]
[[Category: Yamashita, S]]
[[Category: Tomita K]]
[[Category: A-adding enzyme]]
[[Category: Yamashita S]]
[[Category: Cca-adding enzyme]]
[[Category: Rna nucleotidyltransferase]]
[[Category: Transferase-rna complex]]

Latest revision as of 18:24, 8 November 2023

Structure of tRNA-processing enzyme complex 6Structure of tRNA-processing enzyme complex 6

Structural highlights

4x0a is a 2 chain structure with sequence from Aquifex aeolicus VF5 and Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.505Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AATNT_AQUAE tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the terminal adenosine residue to tRNA (PubMed:11701927, PubMed:25914059). Can incorporate CMP into tRNA ending with C74C75 (tRNACC), with very weak efficiency (PubMed:25914059).[1] [2]

Publication Abstract from PubMed

The 3'-terminal CCA (C74C75A76-3') of tRNA is required for protein synthesis. In Aquifex aeolicus, the CCA-3' is synthesized by CC-adding and A-adding enzymes, although in most organisms, CCA is synthesized by a single CCA-adding enzyme. The mechanisms by which the A-adding enzyme adds only A76, but not C74C75, onto tRNA remained elusive. The complex structures of the enzyme with various tRNAs revealed the presence of a single tRNA binding site on the enzyme, with the enzyme measuring the acceptor-TPsiC helix length of tRNA. The 3'-C75 of tRNA lacking A76 can reach the active site and the size and shape of the nucleotide binding pocket at the insertion stage are suitable for ATP. The 3'-C74 of tRNA lacking C75A76 cannot reach the active site, although CTP or ATP can bind the active pocket. Thus, the A-adding enzyme adds only A76, but not C74C75, onto tRNA.

Measurement of Acceptor-TPsiC Helix Length of tRNA for Terminal A76-Addition by A-Adding Enzyme.,Yamashita S, Martinez A, Tomita K Structure. 2015 May 5;23(5):830-42. doi: 10.1016/j.str.2015.03.013. Epub 2015 Apr, 23. PMID:25914059[3]

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

See Also

References

  1. 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
  2. Yamashita S, Martinez A, Tomita K. Measurement of Acceptor-TPsiC Helix Length of tRNA for Terminal A76-Addition by A-Adding Enzyme. Structure. 2015 May 5;23(5):830-42. doi: 10.1016/j.str.2015.03.013. Epub 2015 Apr, 23. PMID:25914059 doi:http://dx.doi.org/10.1016/j.str.2015.03.013
  3. Yamashita S, Martinez A, Tomita K. Measurement of Acceptor-TPsiC Helix Length of tRNA for Terminal A76-Addition by A-Adding Enzyme. Structure. 2015 May 5;23(5):830-42. doi: 10.1016/j.str.2015.03.013. Epub 2015 Apr, 23. PMID:25914059 doi:http://dx.doi.org/10.1016/j.str.2015.03.013

4x0a, resolution 3.50Å

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