4DMG

Thermus thermophilus m5C1942 methyltransferase RlmO

4DMG の概要

• エントリーDOI: 10.2210/pdb4dmg/pdb
• 分子名称: Putative uncharacterized protein TTHA1493, S-ADENOSYLMETHIONINE (3 entities in total)
• 機能のキーワード: rrna, methyltransferase, s-adenosyl-methionine, 23s ribosomal rna, transferase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90199.58

構造登録者

Larsen, H.G.,Rasmussen, A.,Giessing, A.M.B.,Jogl, G.,Kirpekar, F. (登録日: 2012-02-07, 公開日: 2012-06-27, 最終更新日: 2024-02-28)

主引用文献

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

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: 22711535
DOI: 10.1074/jbc.M112.376160

実験手法

X-RAY DIFFRACTION (1.7 Å)