4wc6: Difference between revisions

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<StructureSection load='4wc6' size='340' side='right'caption='[[4wc6]], [[Resolution|resolution]] 3.41&Aring;' scene=''>
<StructureSection load='4wc6' size='340' side='right'caption='[[4wc6]], [[Resolution|resolution]] 3.41&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4wc6]] 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=4WC6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WC6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4wc6]] 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=4WC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WC6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vfg|1vfg]], [[4wby|4wby]], [[4wbz|4wbz]], [[4wc0|4wc0]], [[4wc1|4wc1]], [[4wc2|4wc2]], [[4wc3|4wc3]], [[4wc4|4wc4]], [[4wc5|4wc5]], [[4wc7|4wc7]]</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=4wc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wc6 OCA], [https://pdbe.org/4wc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wc6 RCSB], [https://www.ebi.ac.uk/pdbsum/4wc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wc6 ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wc6 OCA], [http://pdbe.org/4wc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wc6 RCSB], [http://www.ebi.ac.uk/pdbsum/4wc6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wc6 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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__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]]

Revision as of 10:01, 7 April 2023

Structure of tRNA-processing enzyme complex 4Structure of tRNA-processing enzyme complex 4

Structural highlights

4wc6 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.
Ligands:
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

4wc6, resolution 3.41Å

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