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| | ==Crystal structure of Bacillus subtilis TmcAL bound with ATP (SeMet derivative)== | | ==Crystal structure of Bacillus subtilis TmcAL bound with ATP (SeMet derivative)== |
| - | <StructureSection load='5y0n' size='340' side='right' caption='[[5y0n]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='5y0n' size='340' side='right'caption='[[5y0n]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5y0n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y0N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y0N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5y0n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y0N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></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]] 2.302Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B4417_3650 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=5y0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y0n OCA], [https://pdbe.org/5y0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y0n RCSB], [https://www.ebi.ac.uk/pdbsum/5y0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y0n 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=5y0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y0n OCA], [http://pdbe.org/5y0n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y0n RCSB], [http://www.ebi.ac.uk/pdbsum/5y0n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y0n ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TMCAL_BACSU TMCAL_BACSU] Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.[HAMAP-Rule:MF_01539]<ref>PMID:30150682</ref> |
| | <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: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Tomita, K]] | + | [[Category: Large Structures]] |
| - | [[Category: Yamashita, S]] | + | [[Category: Tomita K]] |
| - | [[Category: Acetate ligase]] | + | [[Category: Yamashita S]] |
| - | [[Category: Ligase]]
| + | |
| Structural highlights
Function
TMCAL_BACSU Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.[HAMAP-Rule:MF_01539][1]
Publication Abstract from PubMed
Modification of tRNA anticodons plays a critical role in ensuring accurate translation. N(4)-acetylcytidine (ac(4)C) is present at the anticodon first position (position 34) of bacterial elongator tRNA(Met). Herein, we identified Bacillus subtilis ylbM (renamed tmcAL) as a novel gene responsible for ac(4)C34 formation. Unlike general acetyltransferases that use acetyl-CoA, TmcAL activates an acetate ion to form acetyladenylate and then catalyzes ac(4)C34 formation through a mechanism similar to tRNA aminoacylation. The crystal structure of TmcAL with an ATP analog reveals the molecular basis of ac(4)C34 formation. The DeltatmcAL strain displayed a cold-sensitive phenotype and a strong genetic interaction with tilS that encodes the enzyme responsible for synthesizing lysidine (L) at position 34 of tRNA(Ile) to facilitate AUA decoding. Mistranslation of the AUA codon as Met in the DeltatmcAL strain upon tilS repression suggests that ac(4)C34 modification of tRNA(Met) and L34 modification of tRNA(Ile) act cooperatively to prevent misdecoding of the AUA codon.
Acetate-dependent tRNA acetylation required for decoding fidelity in protein synthesis.,Taniguchi T, Miyauchi K, Sakaguchi Y, Yamashita S, Soma A, Tomita K, Suzuki T Nat Chem Biol. 2018 Nov;14(11):1010-1020. doi: 10.1038/s41589-018-0119-z. Epub, 2018 Aug 27. PMID:30150682[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Taniguchi T, Miyauchi K, Sakaguchi Y, Yamashita S, Soma A, Tomita K, Suzuki T. Acetate-dependent tRNA acetylation required for decoding fidelity in protein synthesis. Nat Chem Biol. 2018 Nov;14(11):1010-1020. doi: 10.1038/s41589-018-0119-z. Epub, 2018 Aug 27. PMID:30150682 doi:http://dx.doi.org/10.1038/s41589-018-0119-z
- ↑ Taniguchi T, Miyauchi K, Sakaguchi Y, Yamashita S, Soma A, Tomita K, Suzuki T. Acetate-dependent tRNA acetylation required for decoding fidelity in protein synthesis. Nat Chem Biol. 2018 Nov;14(11):1010-1020. doi: 10.1038/s41589-018-0119-z. Epub, 2018 Aug 27. PMID:30150682 doi:http://dx.doi.org/10.1038/s41589-018-0119-z
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