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| | <StructureSection load='5axl' size='340' side='right'caption='[[5axl]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='5axl' size='340' side='right'caption='[[5axl]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5axl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35395 Atcc 35395]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AXL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AXL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5axl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans Methanosarcina acetivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AXL 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">[[5axk|5axk]], [[5axm|5axm]], [[5axn|5axn]]</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=5axl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5axl OCA], [https://pdbe.org/5axl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5axl RCSB], [https://www.ebi.ac.uk/pdbsum/5axl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5axl 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=5axl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5axl OCA], [http://pdbe.org/5axl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5axl RCSB], [http://www.ebi.ac.uk/pdbsum/5axl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5axl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A1C7D1G9_9EURY A0A1C7D1G9_9EURY] |
| | <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: Atcc 35395]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kato, K]] | + | [[Category: Methanosarcina acetivorans]] |
| - | [[Category: Kimura, S]] | + | [[Category: Kato K]] |
| - | [[Category: Suzuki, T]] | + | [[Category: Kimura S]] |
| - | [[Category: Yao, M]] | + | [[Category: Suzuki T]] |
| - | [[Category: Yu, J]] | + | [[Category: Yao M]] |
| - | [[Category: Transferase]]
| + | [[Category: Yu J]] |
| Structural highlights
Function
A0A1C7D1G9_9EURY
Publication Abstract from PubMed
Thg1-like protein (TLP) catalyzes the addition of a nucleotide to the 5'-end of truncated transfer RNA (tRNA) species in a Watson-Crick template-dependent manner. The reaction proceeds in two steps: the activation of the 5'-end by adenosine 5'-triphosphate (ATP)/guanosine 5'-triphosphate (GTP), followed by nucleotide addition. Structural analyses of the TLP and its reaction intermediates have revealed the atomic detail of the template-dependent elongation reaction in the 3'-5' direction. The enzyme creates two substrate binding sites for the first- and second-step reactions in the vicinity of one reaction center consisting of two Mg(2+) ions, and the two reactions are executed at the same reaction center in a stepwise fashion. When the incoming nucleotide is bound to the second binding site with Watson-Crick hydrogen bonds, the 3'-OH of the incoming nucleotide and the 5'-triphosphate of the tRNA are moved to the reaction center where the first reaction has occurred. That the 3'-5' elongation enzyme performs this elaborate two-step reaction in one catalytic center suggests that these two reactions have been inseparable throughout the process of protein evolution. Although TLP and Thg1 have similar tetrameric organization, the tRNA binding mode of TLP is different from that of Thg1, a tRNA(His)-specific G-1 addition enzyme. Each tRNA(His) binds to three of the four Thg1 tetramer subunits, whereas in TLP, tRNA only binds to a dimer interface and the elongation reaction is terminated by measuring the accepter stem length through the flexible beta-hairpin. Furthermore, mutational analyses show that tRNA(His) is bound to TLP in a similar manner as Thg1, thus indicating that TLP has a dual binding mode.
Template-dependent nucleotide addition in the reverse (3'-5') direction by Thg1-like protein.,Kimura S, Suzuki T, Chen M, Kato K, Yu J, Nakamura A, Tanaka I, Yao M Sci Adv. 2016 Mar 25;2(3):e1501397. doi: 10.1126/sciadv.1501397. eCollection 2016, Mar. PMID:27051866[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kimura S, Suzuki T, Chen M, Kato K, Yu J, Nakamura A, Tanaka I, Yao M. Template-dependent nucleotide addition in the reverse (3'-5') direction by Thg1-like protein. Sci Adv. 2016 Mar 25;2(3):e1501397. doi: 10.1126/sciadv.1501397. eCollection 2016, Mar. PMID:27051866 doi:http://dx.doi.org/10.1126/sciadv.1501397
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