Structural highlights5b4e is a 1 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 2.698Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
FunctionTTUA_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).[1] [2]
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
- ↑ 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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