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3ote

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Current revision (10:36, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3ote' size='340' side='right'caption='[[3ote]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
<StructureSection load='3ote' size='340' side='right'caption='[[3ote]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ote]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3OTE FirstGlance]. <br>
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<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>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3otb|3otb]], [[3otc|3otc]], [[3otd|3otd]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.56&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ICF45, THG1L ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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'>[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>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<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&reg;/PubMed&reg;, 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>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Doublie, S]]
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[[Category: Doublie S]]
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[[Category: Eckenroth, B E]]
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[[Category: Eckenroth BE]]
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[[Category: Hyde, S J]]
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[[Category: Hyde SJ]]
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[[Category: Catalytic carboxylate]]
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[[Category: Guanylyltransferase]]
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[[Category: Polymerase-like palm domain]]
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[[Category: Transferase]]
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Current revision

Crystal structure of human tRNAHis guanylyltransferase (Thg1)- Native I

PDB ID 3ote

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