3P9N

Rv2966c of M. tuberculosis is a RsmD-like methyltransferase

3P9N の概要

• エントリーDOI: 10.2210/pdb3p9n/pdb
• 分子名称: POSSIBLE METHYLTRANSFERASE (METHYLASE), ACETATE ION (3 entities in total)
• 機能のキーワード: rv2966c, adomet binding, rna methylase, rsmd, sam-fold, rna methyltransferase, transferase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20032.66

構造登録者

Kumar, A.,Malhotra, K.,Saigal, K.,Sinha, K.M.,Taneja, B. (登録日: 2010-10-18, 公開日: 2011-04-06, 最終更新日: 2023-11-01)

主引用文献

Kumar, A.,Saigal, K.,Malhotra, K.,Sinha, K.M.,Taneja, B.
Structural and functional characterization of Rv2966c protein reveals an RsmD-like methyltransferase from Mycobacterium tuberculosis and the role of its N-terminal domain in target recognition
J.Biol.Chem., 286:19652-19661, 2011

PubMed Abstract: Nine of ten methylated nucleotides of Escherichia coli 16 S rRNA are conserved in Mycobacterium tuberculosis. All the 10 different methyltransferases are known in E. coli, whereas only TlyA and GidB have been identified in mycobacteria. Here we have identified Rv2966c of M. tuberculosis as an ortholog of RsmD protein of E. coli. We have shown that rv2966c can complement rsmD-deleted E. coli cells. Recombinant Rv2966c can use 30 S ribosomes purified from rsmD-deleted E. coli as substrate and methylate G966 of 16 S rRNA in vitro. Structure determination of the protein shows the protein to be a two-domain structure with a short hairpin domain at the N terminus and a C-terminal domain with the S-adenosylmethionine-MT-fold. We show that the N-terminal hairpin is a minimalist functional domain that helps Rv2966c in target recognition. Deletion of the N-terminal domain prevents binding to nucleic acid substrates, and the truncated protein fails to carry out the m(2)G966 methylation on 16 S rRNA. The N-terminal domain also binds DNA efficiently, a property that may be utilized under specific conditions of cellular growth.

PubMed: 21474448
DOI: 10.1074/jbc.M110.200428

実験手法

X-RAY DIFFRACTION (1.9 Å)