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| | <StructureSection load='1ou5' size='340' side='right'caption='[[1ou5]], [[Resolution|resolution]] 3.40Å' scene=''> | | <StructureSection load='1ou5' size='340' side='right'caption='[[1ou5]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ou5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OU5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OU5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ou5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OU5 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1miv|1miv]], [[1miw|1miw]], [[1miy|1miy]]</div></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]] 3.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hMtCCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1ou5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ou5 OCA], [https://pdbe.org/1ou5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ou5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ou5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ou5 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ou5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ou5 OCA], [http://pdbe.org/1ou5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ou5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ou5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ou5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TRNT1_HUMAN TRNT1_HUMAN]] Isoform 1: Adds and repairs the conserved 3'-CCA sequence necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates.<ref>PMID:17204286</ref> Isoform 2: Adds 2 C residues (CC-) to the 3' terminus of tRNA molecules instead of a complete CCA end as isoform 1 does (in vitro).<ref>PMID:17204286</ref> | + | [https://www.uniprot.org/uniprot/TRNT1_HUMAN TRNT1_HUMAN] Isoform 1: Adds and repairs the conserved 3'-CCA sequence necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates.<ref>PMID:17204286</ref> Isoform 2: Adds 2 C residues (CC-) to the 3' terminus of tRNA molecules instead of a complete CCA end as isoform 1 does (in vitro).<ref>PMID:17204286</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/1ou5_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/1ou5_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Augustin, M A]] | + | [[Category: Augustin MA]] |
| - | [[Category: Betat, H]] | + | [[Category: Betat H]] |
| - | [[Category: Huber, R]] | + | [[Category: Huber R]] |
| - | [[Category: Moerl, M]] | + | [[Category: Moerl M]] |
| - | [[Category: Reichert, A S]] | + | [[Category: Reichert AS]] |
| - | [[Category: Steegborn, C]] | + | [[Category: Steegborn C]] |
| - | [[Category: Nucleotidyltransferase]]
| + | |
| - | [[Category: Polymerase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Translation]]
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| - | [[Category: Trna]]
| + | |
| Structural highlights
Function
TRNT1_HUMAN Isoform 1: Adds and repairs the conserved 3'-CCA sequence necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates.[1] Isoform 2: Adds 2 C residues (CC-) to the 3' terminus of tRNA molecules instead of a complete CCA end as isoform 1 does (in vitro).[2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
All tRNA molecules carry the invariant sequence CCA at their 3'-terminus for amino acid attachment. The post-transcriptional addition of CCA is carried out by ATP(CTP):tRNA nucleotidyltransferase, also called CCase. This enzyme catalyses a unique template-independent but sequence-specific nucleotide polymerization reaction. In order to reveal the molecular mechanism of this activity, we solved the crystal structure of human CCase by single isomorphous replacement. The structure reveals a four domain architecture with a cluster of conserved residues forming a positively charged cleft between the first two domains. Structural homology of the N-terminal CCase domain to other nucleotidyltransferases could be exploited for modeling a tRNA-substrate complex. The model places the tRNA 3'-end into the N-terminal nucleotidyltransferase site, close to a patch of conserved residues that provide the binding sites for CTP and ATP. Based on our results, we introduce a corkscrew model for CCA addition that includes a fixed active site and a traveling tRNA-binding region formed by flexible parts of the protein.
Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization.,Augustin MA, Reichert AS, Betat H, Huber R, Morl M, Steegborn C J Mol Biol. 2003 May 16;328(5):985-94. PMID:12729736[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lizano E, Schuster J, Muller M, Kelso J, Morl M. A splice variant of the human CCA-adding enzyme with modified activity. J Mol Biol. 2007 Mar 2;366(4):1258-65. Epub 2006 Dec 12. PMID:17204286 doi:http://dx.doi.org/10.1016/j.jmb.2006.12.016
- ↑ Lizano E, Schuster J, Muller M, Kelso J, Morl M. A splice variant of the human CCA-adding enzyme with modified activity. J Mol Biol. 2007 Mar 2;366(4):1258-65. Epub 2006 Dec 12. PMID:17204286 doi:http://dx.doi.org/10.1016/j.jmb.2006.12.016
- ↑ Augustin MA, Reichert AS, Betat H, Huber R, Morl M, Steegborn C. Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization. J Mol Biol. 2003 May 16;328(5):985-94. PMID:12729736
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