5TWK

Crystal Structure of RlmH in Complex with Sinefungin

5TWK の概要

• エントリーDOI: 10.2210/pdb5twk/pdb
• 関連するPDBエントリー: 5TWJ
• 分子名称: Ribosomal RNA large subunit methyltransferase H, SINEFUNGIN (3 entities in total)
• 機能のキーワード: sinefungin, rna methyltransferase, spout, pseudouridine, helix 69, transferase, transferase-antibiotic complex, transferase/antibiotic
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 74697.99

構造登録者

Koh, C.S.,Madireddy, R.,Beane, T.J.,Zamore, P.D.,Korostelev, A.A. (登録日: 2016-11-14, 公開日: 2017-05-03, 最終更新日: 2023-10-04)

主引用文献

Koh, C.S.,Madireddy, R.,Beane, T.J.,Zamore, P.D.,Korostelev, A.A.
Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine.
Sci Rep, 7:969-969, 2017

PubMed Abstract: Eubacterial ribosomal large-subunit methyltransferase H (RlmH) methylates 23S ribosomal RNA pseudouridine 1915 (Ψ1915), which lies near the ribosomal decoding center. The smallest member of the SPOUT superfamily of methyltransferases, RlmH lacks the RNA recognition domain found in larger methyltransferases. The catalytic mechanism of RlmH enzyme is unknown. Here, we describe the structures of RlmH bound to S-adenosyl-methionine (SAM) and the methyltransferase inhibitor sinefungin. Our structural and biochemical studies reveal catalytically essential residues in the dimer-mediated asymmetrical active site. One monomer provides the SAM-binding site, whereas the conserved C-terminal tail of the second monomer provides residues essential for catalysis. Our findings elucidate the mechanism by which a small protein dimer assembles a functionally asymmetric architecture.

PubMed: 28428565
DOI: 10.1038/s41598-017-01186-5

実験手法

X-RAY DIFFRACTION (2.1 Å)