3otd
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of human tRNAHis guanylyltransferase (Thg1)- NaI derivative== | |
| - | + | <StructureSection load='3otd' size='340' side='right' caption='[[3otd]], [[Resolution|resolution]] 2.28Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3otd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycta Mycta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OTD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OTD FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3otb|3otb]], [[3otc|3otc]], [[3ote|3ote]]</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=419947 MYCTA])</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=3otd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3otd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3otd RCSB], [http://www.ebi.ac.uk/pdbsum/3otd PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Mycta]] | [[Category: Mycta]] | ||
| - | [[Category: Doublie, S | + | [[Category: Doublie, S]] |
| - | [[Category: Eckenroth, B E | + | [[Category: Eckenroth, B E]] |
| - | [[Category: Hyde, S J | + | [[Category: Hyde, S J]] |
[[Category: Catalytic carboxylate]] | [[Category: Catalytic carboxylate]] | ||
[[Category: Guanylyltransferase]] | [[Category: Guanylyltransferase]] | ||
[[Category: Polymerase-like palm domain]] | [[Category: Polymerase-like palm domain]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 17:40, 25 December 2014
Crystal structure of human tRNAHis guanylyltransferase (Thg1)- NaI derivative
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