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| | <StructureSection load='5ztb' size='340' side='right'caption='[[5ztb]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='5ztb' size='340' side='right'caption='[[5ztb]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ztb]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZTB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZTB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ztb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZTB 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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/tRNA-5-methyluridine(54)_2-sulfurtransferase tRNA-5-methyluridine(54) 2-sulfurtransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.15 2.8.1.15] </span></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5ztb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ztb OCA], [http://pdbe.org/5ztb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ztb RCSB], [http://www.ebi.ac.uk/pdbsum/5ztb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ztb 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=5ztb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ztb OCA], [https://pdbe.org/5ztb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ztb RCSB], [https://www.ebi.ac.uk/pdbsum/5ztb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ztb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TTUB_THET2 TTUB_THET2]] Required for the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T) (PubMed:16547008, PubMed:28439027). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is essential for cell growth at high temperatures (PubMed:16547008). Thiocarboxylated TtuB functions as the sulfur donor in the sulfurtransferase reaction catalyzed by TtuA (PubMed:28439027, PubMed:19037260). TtuB also functions as a protein modifier covalently attached to lysine residues of the target proteins TtuA and TtuC (PubMed:22467871). TtuB conjugation might play a regulatory role to ensure appropriate sulfur transfer in cells (PubMed:22467871).<ref>PMID:16547008</ref> <ref>PMID:19037260</ref> <ref>PMID:22467871</ref> <ref>PMID:28439027</ref> [[http://www.uniprot.org/uniprot/TTUA_THET2 TTUA_THET2]] Catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T) (PubMed:16547008, PubMed:28439027). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is required for cell growth at high temperatures (PubMed:16547008). TtuA transfers the S atom from the thiocarboxylated C-terminus of TtuB to tRNA (PubMed:28439027).<ref>PMID:16547008</ref> <ref>PMID:28439027</ref> | + | [https://www.uniprot.org/uniprot/TTUB_THET2 TTUB_THET2] Required for the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T) (PubMed:16547008, PubMed:28439027). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is essential for cell growth at high temperatures (PubMed:16547008). Thiocarboxylated TtuB functions as the sulfur donor in the sulfurtransferase reaction catalyzed by TtuA (PubMed:28439027, PubMed:19037260). TtuB also functions as a protein modifier covalently attached to lysine residues of the target proteins TtuA and TtuC (PubMed:22467871). TtuB conjugation might play a regulatory role to ensure appropriate sulfur transfer in cells (PubMed:22467871).<ref>PMID:16547008</ref> <ref>PMID:19037260</ref> <ref>PMID:22467871</ref> <ref>PMID:28439027</ref> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, M]] | + | [[Category: Thermus thermophilus HB27]] |
| - | [[Category: Narai, S]] | + | [[Category: Chen M]] |
| - | [[Category: Tanaka, Y]] | + | [[Category: Narai S]] |
| - | [[Category: Yao, M]] | + | [[Category: Tanaka Y]] |
| - | [[Category: Complex]]
| + | [[Category: Yao M]] |
| - | [[Category: Iron-sulfur cluster]]
| + | |
| - | [[Category: Rna binding protein]]
| + | |
| - | [[Category: Rna binding protein-transferase complex]]
| + | |
| - | [[Category: Sulfur transfer]]
| + | |
| - | [[Category: Trna binding protein]]
| + | |
| Structural highlights
5ztb is a 6 chain structure with sequence from Thermus thermophilus HB27. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.2Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
TTUB_THET2 Required for the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T) (PubMed:16547008, PubMed:28439027). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is essential for cell growth at high temperatures (PubMed:16547008). Thiocarboxylated TtuB functions as the sulfur donor in the sulfurtransferase reaction catalyzed by TtuA (PubMed:28439027, PubMed:19037260). TtuB also functions as a protein modifier covalently attached to lysine residues of the target proteins TtuA and TtuC (PubMed:22467871). TtuB conjugation might play a regulatory role to ensure appropriate sulfur transfer in cells (PubMed:22467871).[1] [2] [3] [4]
References
- ↑ Shigi N, Sakaguchi Y, Suzuki T, Watanabe K. Identification of two tRNA thiolation genes required for cell growth at extremely high temperatures. J Biol Chem. 2006 May 19;281(20):14296-306. doi: 10.1074/jbc.M511675200. Epub, 2006 Mar 17. PMID:16547008 doi:http://dx.doi.org/10.1074/jbc.M511675200
- ↑ Shigi N, Sakaguchi Y, Asai S, Suzuki T, Watanabe K. Common thiolation mechanism in the biosynthesis of tRNA thiouridine and sulphur-containing cofactors. EMBO J. 2008 Dec 17;27(24):3267-78. doi: 10.1038/emboj.2008.246. Epub 2008 Nov, 27. PMID:19037260 doi:http://dx.doi.org/10.1038/emboj.2008.246
- ↑ Shigi N. Posttranslational modification of cellular proteins by a ubiquitin-like protein in bacteria. J Biol Chem. 2012 May 18;287(21):17568-77. doi: 10.1074/jbc.M112.359844. Epub, 2012 Mar 30. PMID:22467871 doi:http://dx.doi.org/10.1074/jbc.M112.359844
- ↑ Chen M, Asai SI, Narai S, Nambu S, Omura N, Sakaguchi Y, Suzuki T, Ikeda-Saito M, Watanabe K, Yao M, Shigi N, Tanaka Y. Biochemical and structural characterization of oxygen-sensitive 2-thiouridine synthesis catalyzed by an iron-sulfur protein TtuA. Proc Natl Acad Sci U S A. 2017 Apr 24. pii: 201615585. doi:, 10.1073/pnas.1615585114. PMID:28439027 doi:http://dx.doi.org/10.1073/pnas.1615585114
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