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5ztb
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Sulfurtransferase== | |
| - | + | <StructureSection load='5ztb' size='340' side='right'caption='[[5ztb]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == 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> | |
| - | + | </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> | |
| - | [[Category: | + | <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='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> | ||
| + | </table> | ||
| + | == 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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen, M]] | ||
[[Category: Narai, S]] | [[Category: Narai, S]] | ||
| - | [[Category: | + | [[Category: Tanaka, Y]] |
[[Category: Yao, M]] | [[Category: Yao, M]] | ||
| - | [[Category: | + | [[Category: Complex]] |
| + | [[Category: Iron-sulfur cluster]] | ||
| + | [[Category: Rna binding protein]] | ||
| + | [[Category: Rna binding protein-transferase complex]] | ||
| + | [[Category: Sulfur transfer]] | ||
| + | [[Category: Trna binding protein]] | ||
Revision as of 05:24, 12 June 2019
Structure of Sulfurtransferase
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