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| | ==Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein in complex with GTP== | | ==Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein in complex with GTP== |
| - | <StructureSection load='4kgk' size='340' side='right' caption='[[4kgk]], [[Resolution|resolution]] 2.95Å' scene=''> | + | <StructureSection load='4kgk' size='340' side='right'caption='[[4kgk]], [[Resolution|resolution]] 2.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kgk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_israelensis_atcc_35646 Bacillus thuringiensis serovar israelensis atcc 35646]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KGK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KGK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kgk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_israelensis_ATCC_35646 Bacillus thuringiensis serovar israelensis ATCC 35646]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KGK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kgm|4kgm]]</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=4kgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgk OCA], [https://pdbe.org/4kgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kgk RCSB], [https://www.ebi.ac.uk/pdbsum/4kgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kgk ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RBTH_06728 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=339854 Bacillus thuringiensis serovar israelensis ATCC 35646])</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=4kgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgk OCA], [http://pdbe.org/4kgk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kgk RCSB], [http://www.ebi.ac.uk/pdbsum/4kgk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kgk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q3F0V8_BACTI Q3F0V8_BACTI] |
| | <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: Bacillus thuringiensis serovar israelensis atcc 35646]] | + | [[Category: Bacillus thuringiensis serovar israelensis ATCC 35646]] |
| - | [[Category: Doublie, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Eckenroth, B E]] | + | [[Category: Doublie S]] |
| - | [[Category: Hyde, S J]]
| + | [[Category: Eckenroth BE]] |
| - | [[Category: Jackman, J E]] | + | [[Category: Hyde SJ]] |
| - | [[Category: Rao, B S]] | + | [[Category: Jackman JE]] |
| - | [[Category: Atp binding]] | + | [[Category: Rao BS]] |
| - | [[Category: Gtp binding]] | + | |
| - | [[Category: Polymerase-like catalytic domain]]
| + | |
| - | [[Category: Transferase]]
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| - | [[Category: Trna binding]]
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| Structural highlights
Function
Q3F0V8_BACTI
Publication Abstract from PubMed
All nucleotide polymerases and transferases catalyze nucleotide addition in a 5' to 3' direction. In contrast, tRNA(His) guanylyltransferase (Thg1) enzymes catalyze the unusual reverse addition (3' to 5') of nucleotides to polynucleotide substrates. In eukaryotes, Thg1 enzymes use the 3'-5' addition activity to add G-1 to the 5'-end of tRNA(His), a modification required for efficient aminoacylation of the tRNA by the histidyl-tRNA synthetase. Thg1-like proteins (TLPs) are found in Archaea, Bacteria, and mitochondria and are biochemically distinct from their eukaryotic Thg1 counterparts TLPs catalyze 5'-end repair of truncated tRNAs and act on a broad range of tRNA substrates instead of exhibiting strict specificity for tRNA(His). Taken together, these data suggest that TLPs function in distinct biological pathways from the tRNA(His) maturation pathway, perhaps in tRNA quality control. Here we present the first crystal structure of a TLP, from the gram-positive soil bacterium Bacillus thuringiensis (BtTLP). The enzyme is a tetramer like human THG1, with which it shares substantial structural similarity. Catalysis of the 3'-5' reaction with 5'-monophosphorylated tRNA necessitates first an activation step, generating a 5'-adenylylated intermediate prior to a second nucleotidyl transfer step, in which a nucleotide is transferred to the tRNA 5'-end. Consistent with earlier characterization of human THG1, we observed distinct binding sites for the nucleotides involved in these two steps of activation and nucleotidyl transfer. A BtTLP complex with GTP reveals new interactions with the GTP nucleotide in the activation site that were not evident from the previously solved structure. Moreover, the BtTLP-ATP structure allows direct observation of ATP in the activation site for the first time. The BtTLP structural data, combined with kinetic analysis of selected variants, provide new insight into the role of key residues in the activation step.
Structural Studies of a Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein, with Nucleotide in the Activation and Nucleotidyl Transfer Sites.,Hyde SJ, Rao BS, Eckenroth BE, Jackman JE, Doublie S PLoS One. 2013 Jul 3;8(7):e67465. doi: 10.1371/journal.pone.0067465. Print 2013. PMID:23844012[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hyde SJ, Rao BS, Eckenroth BE, Jackman JE, Doublie S. Structural Studies of a Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein, with Nucleotide in the Activation and Nucleotidyl Transfer Sites. PLoS One. 2013 Jul 3;8(7):e67465. doi: 10.1371/journal.pone.0067465. Print 2013. PMID:23844012 doi:10.1371/journal.pone.0067465
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