2YXL

Crystal Structure of PH0851

2YXL の概要

• エントリーDOI: 10.2210/pdb2yxl/pdb
• 分子名称: 450aa long hypothetical fmu protein, SINEFUNGIN (3 entities in total)
• 機能のキーワード: fmu-homolog, methyltransferase, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, transferase
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52100.49

構造登録者

Hikida, Y.,Kuratani, M.,Bessho, Y.,Ishii, R.,Sekine, S.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2007-04-26, 公開日: 2008-04-29, 最終更新日: 2023-10-25)

主引用文献

Hikida, Y.,Kuratani, M.,Bessho, Y.,Sekine, S.,Yokoyama, S.
Structure of an archaeal homologue of the bacterial Fmu/RsmB/RrmB rRNA cytosine 5-methyltransferase
Acta Crystallogr.,Sect.D, 66:1301-1307, 2010

PubMed Abstract: One of the modified nucleosides that frequently occurs in rRNAs and tRNAs is 5-methylcytidine (m⁵C). Escherichia coli Fmu/RsmB/RrmB is an S-adenosyl-L-methionine (AdoMet)-dependent methyltransferase that forms m⁵C967 in 16S rRNA. Fmu/RsmB/RrmB homologues exist not only in bacteria but also in archaea and eukarya and constitute a large orthologous group in the RNA:m⁵C methyltransferase family. In the present study, the crystal structure of a homologue of E. coli Fmu/RsmB/RrmB from the archaeon Pyrococcus horikoshii (PH0851) complexed with an AdoMet analogue was determined at 2.55 Å resolution. The structure and sequence of the C-terminal catalytic domain are highly conserved compared with those of E. coli Fmu/RsmB/RrmB. In contrast, the sequence of the N-terminal domain is negligibly conserved between the bacterial and archaeal subfamilies. Nevertheless, the N-terminal domains of PH0851 and E. coli Fmu/RsmB/RrmB are both α-helical and adopt a similar topology. Next to the AdoMet-binding site, a positively charged cleft is formed between the N- and C-terminal domains. This cleft is conserved in the archaeal PH0851 homologues and seems to be suitable for binding the RNA substrate.

PubMed: 21123870
DOI: 10.1107/S0907444910037558

実験手法

X-RAY DIFFRACTION (2.55 Å)