5MKP
Non redox thiolation in transfer RNAs occuring via sulfur activation by a [4Fe-4S] cluster
Summary for 5MKP
| Entry DOI | 10.2210/pdb5mkp/pdb |
| Related | 3VRH |
| Descriptor | PH0300, ZINC ION, Fe4 H S5, ... (4 entities in total) |
| Functional Keywords | ttua, [4fe-5s], sulfur insertion, trna modification, thiolation reaction, iron-sulfur cluster, rna |
| Biological source | Pyrococcus horikoshii OT3 |
| Total number of polymer chains | 1 |
| Total formula weight | 36438.41 |
| Authors | Arragain, S.,Bimai, O.,Legrand, P.,Golinelli-Pimpaneau, B. (deposition date: 2016-12-05, release date: 2017-06-14, Last modification date: 2024-01-17) |
| Primary citation | Arragain, S.,Bimai, O.,Legrand, P.,Caillat, S.,Ravanat, J.L.,Touati, N.,Binet, L.,Atta, M.,Fontecave, M.,Golinelli-Pimpaneau, B. Nonredox thiolation in tRNA occurring via sulfur activation by a [4Fe-4S] cluster. Proc. Natl. Acad. Sci. U.S.A., 114:7355-7360, 2017 Cited by PubMed Abstract: Sulfur is present in several nucleosides within tRNAs. In particular, thiolation of the universally conserved methyl-uridine at position 54 stabilizes tRNAs from thermophilic bacteria and hyperthermophilic archaea and is required for growth at high temperature. The simple nonredox substitution of the C2-uridine carbonyl oxygen by sulfur is catalyzed by tRNA thiouridine synthetases called TtuA. Spectroscopic, enzymatic, and structural studies indicate that TtuA carries a catalytically essential [4Fe-4S] cluster and requires ATP for activity. A series of crystal structures shows that () the cluster is ligated by only three cysteines that are fully conserved, allowing the fourth unique iron to bind a small ligand, such as exogenous sulfide, and () the ATP binding site, localized thanks to a protein-bound AMP molecule, a reaction product, is adjacent to the cluster. A mechanism for tRNA sulfuration is suggested, in which the unique iron of the catalytic cluster serves to bind exogenous sulfide, thus acting as a sulfur carrier. PubMed: 28655838DOI: 10.1073/pnas.1700902114 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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