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| | ==Crystal structure of human tRNAHis guanylyltransferase (Thg1)- Native I== | | ==Crystal structure of human tRNAHis guanylyltransferase (Thg1)- Native I== |
| - | <StructureSection load='3ote' size='340' side='right' caption='[[3ote]], [[Resolution|resolution]] 2.56Å' scene=''> | + | <StructureSection load='3ote' size='340' side='right'caption='[[3ote]], [[Resolution|resolution]] 2.56Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ote]] 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=3OTE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OTE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ote]] 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=3OTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OTE FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3otb|3otb]], [[3otc|3otc]], [[3otd|3otd]]</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]] 2.56Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ICF45, THG1L ([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=3ote FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ote OCA], [https://pdbe.org/3ote PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ote RCSB], [https://www.ebi.ac.uk/pdbsum/3ote PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ote 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=3ote FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ote OCA], [http://pdbe.org/3ote PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ote RCSB], [http://www.ebi.ac.uk/pdbsum/3ote PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ote ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/THG1_HUMAN THG1_HUMAN]] Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is essential for proper recognition of the tRNA and for the fidelity of protein synthesis.<ref>PMID:21059936</ref> | + | [https://www.uniprot.org/uniprot/THG1_HUMAN THG1_HUMAN] Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is essential for proper recognition of the tRNA and for the fidelity of protein synthesis.<ref>PMID:21059936</ref> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | All known DNA and RNA polymerases catalyze the formation of phosphodiester bonds in a 5' to 3' direction, suggesting this property is a fundamental feature of maintaining and dispersing genetic information. The tRNA(His) guanylyltransferase (Thg1) is a member of a unique enzyme family whose members catalyze an unprecedented reaction in biology: 3'-5' addition of nucleotides to nucleic acid substrates. The 2.3-A crystal structure of human THG1 (hTHG1) reported here shows that, despite the lack of sequence similarity, hTHG1 shares unexpected structural homology with canonical 5'-3' DNA polymerases and adenylyl/guanylyl cyclases, two enzyme families known to use a two-metal-ion mechanism for catalysis. The ability of the same structural architecture to catalyze both 5'-3' and 3'-5' reactions raises important questions concerning selection of the 5'-3' mechanism during the evolution of nucleotide polymerases.
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| - | tRNAHis guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases.,Hyde SJ, Eckenroth BE, Smith BA, Eberley WA, Heintz NH, Jackman JE, Doublie S Proc Natl Acad Sci U S A. 2010 Nov 8. PMID:21059936<ref>PMID:21059936</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3ote" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Doublie, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Eckenroth, B E]] | + | [[Category: Doublie S]] |
| - | [[Category: Hyde, S J]]
| + | [[Category: Eckenroth BE]] |
| - | [[Category: Catalytic carboxylate]] | + | [[Category: Hyde SJ]] |
| - | [[Category: Guanylyltransferase]] | + | |
| - | [[Category: Polymerase-like palm domain]]
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| - | [[Category: Transferase]]
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