4DMG
Thermus thermophilus m5C1942 methyltransferase RlmO
Summary for 4DMG
| Entry DOI | 10.2210/pdb4dmg/pdb |
| Descriptor | Putative uncharacterized protein TTHA1493, S-ADENOSYLMETHIONINE (3 entities in total) |
| Functional Keywords | rrna, methyltransferase, s-adenosyl-methionine, 23s ribosomal rna, transferase |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 2 |
| Total formula weight | 90199.58 |
| Authors | Larsen, H.G.,Rasmussen, A.,Giessing, A.M.B.,Jogl, G.,Kirpekar, F. (deposition date: 2012-02-07, release date: 2012-06-27, Last modification date: 2024-02-28) |
| Primary citation | Larsen, L.H.,Rasmussen, A.,Giessing, A.M.,Jogl, G.,Kirpekar, F. Identification and Characterization of the Thermus thermophilus 5-Methylcytidine (m5C) Methyltransferase Modifying 23 S Ribosomal RNA (rRNA) Base C1942. J.Biol.Chem., 287:27593-27600, 2012 Cited by PubMed Abstract: Methylation of cytidines at carbon-5 is a common posttranscriptional RNA modification encountered across all domains of life. Here, we characterize the modifications of C1942 and C1962 in Thermus thermophilus 23 S rRNA as 5-methylcytidines (m(5)C) and identify the two associated methyltransferases. The methyltransferase modifying C1942, named RlmO, has not been characterized previously. RlmO modifies naked 23 S rRNA, but not the assembled 50 S subunit or 70 S ribosomes. The x-ray crystal structure of this enzyme in complex with the S-adenosyl-l-methionine cofactor at 1.7 Å resolution confirms that RlmO is structurally related to other m(5)C rRNA methyltransferases. Key residues in the active site are located similar to the further distant 5-methyluridine methyltransferase RlmD, suggestive of a similar enzymatic mechanism. RlmO homologues are primarily found in mesophilic bacteria related to T. thermophilus. In accordance, we find that growth of the T. thermophilus strain with an inactivated C1942 methyltransferase gene is not compromised at non-optimal temperatures. PubMed: 22711535DOI: 10.1074/jbc.M112.376160 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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