3RFA

X-ray structure of RlmN from Escherichia coli in complex with S-adenosylmethionine

3RFA の概要

• エントリーDOI: 10.2210/pdb3rfa/pdb
• 関連するPDBエントリー: 3RF9
• 分子名称: Ribosomal RNA large subunit methyltransferase N, IRON/SULFUR CLUSTER, S-ADENOSYLMETHIONINE, ... (4 entities in total)
• 機能のキーワード: radical sam, s-adenosylmethionine, iron sulfur cluster, methyltransferase, oxidoreductase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm (Potential): P36979
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92157.85

構造登録者

Boal, A.K.,Grove, T.L.,McLaughlin, M.I.,Yennawar, N.,Booker, S.J.,Rosenzweig, A.C. (登録日: 2011-04-05, 公開日: 2011-05-11, 最終更新日: 2024-10-30)

主引用文献

Boal, A.K.,Grove, T.L.,McLaughlin, M.I.,Yennawar, N.H.,Booker, S.J.,Rosenzweig, A.C.
Structural basis for methyl transfer by a radical SAM enzyme.
Science, 332:1089-1092, 2011

PubMed Abstract: The radical S-adenosyl-L-methionine (SAM) enzymes RlmN and Cfr methylate 23S ribosomal RNA, modifying the C2 or C8 position of adenosine 2503. The methyl groups are installed by a two-step sequence involving initial methylation of a conserved Cys residue (RlmN Cys(355)) by SAM. Methyl transfer to the substrate requires reductive cleavage of a second equivalent of SAM. Crystal structures of RlmN and RlmN with SAM show that a single molecule of SAM coordinates the [4Fe-4S] cluster. Residue Cys(355) is S-methylated and located proximal to the SAM methyl group, suggesting the SAM that is involved in the initial methyl transfer binds at the same site. Thus, RlmN accomplishes its complex reaction with structural economy, harnessing the two most important reactivities of SAM within a single site.

PubMed: 21527678
DOI: 10.1126/science.1205358

実験手法

X-RAY DIFFRACTION (2.05 Å)