5AP8

Structure of the SAM-dependent rRNA:acp-transferase Tsr3 from S. solfataricus

5AP8 の概要

• エントリーDOI: 10.2210/pdb5ap8/pdb
• 関連するPDBエントリー: 5APG
• 分子名称: TSR3 (2 entities in total)
• 機能のキーワード: transferase, s-adenosylmethionine dependent 3-amino-3-carboxypropyl transferase, rrna, pseudouridine, sam, spout-fold
• 由来する生物種: SULFOLOBUS SOLFATARICUS
• 細胞内の位置: Cytoplasm : Q9UWV6
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 57691.18

構造登録者

Wurm, J.P.,Immer, C.,Pogoryelov, D.,Meyer, B.,Koetter, P.,Entian, K.-D.,Woehnert, J. (登録日: 2015-09-14, 公開日: 2016-04-27, 最終更新日: 2024-05-08)

主引用文献

Entian, K.-D.,Immer, C.,Koetter, P.,Lafontaine, D.,Britter, M.,Pogoryelov, D.,Sharma, S.,Wohnert, J.,Wurm, J.P.
Ribosome Biogenesis Factor Tsr3 is the Aminocarboxypropyl Transferase Responsible for 18S Rrna Hypermodification in Yeast and Humans
Nucleic Acids Res., 44:4304-, 2016

PubMed Abstract: The chemically most complex modification in eukaryotic rRNA is the conserved hypermodified nucleotide N1-methyl-N3-aminocarboxypropyl-pseudouridine (m(1)acp(3)Ψ) located next to the P-site tRNA on the small subunit 18S rRNA. While S-adenosylmethionine was identified as the source of the aminocarboxypropyl (acp) group more than 40 years ago the enzyme catalyzing the acp transfer remained elusive. Here we identify the cytoplasmic ribosome biogenesis protein Tsr3 as the responsible enzyme in yeast and human cells. In functionally impaired Tsr3-mutants, a reduced level of acp modification directly correlates with increased 20S pre-rRNA accumulation. The crystal structure of archaeal Tsr3 homologs revealed the same fold as in SPOUT-class RNA-methyltransferases but a distinct SAM binding mode. This unique SAM binding mode explains why Tsr3 transfers the acp and not the methyl group of SAM to its substrate. Structurally, Tsr3 therefore represents a novel class of acp transferase enzymes.

PubMed: 27084949
DOI: 10.1093/NAR/GKW244

実験手法

X-RAY DIFFRACTION (2.246 Å)