3RC8

Human Mitochondrial Helicase Suv3 in Complex with Short RNA Fragment

3RC8 の概要

• エントリーDOI: 10.2210/pdb3rc8/pdb
• 関連するPDBエントリー: 3RC3
• 分子名称: ATP-dependent RNA helicase SUPV3L1, mitochondrial, RNA fragment (2 entities in total)
• 機能のキーワード: helicaase, suv3, mitochondria, rna, helicase, hydrolase-rna complex, hydrolase/rna
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q8IYB8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77897.49

構造登録者

Dauter, Z.,Jedrzejczak, R.,Dauter, M.,Wang, J.,Szczesny, R.,Stepien, P. (登録日: 2011-03-30, 公開日: 2011-05-11, 最終更新日: 2023-09-13)

主引用文献

Jedrzejczak, R.,Wang, J.,Dauter, M.,Szczesny, R.J.,Stepien, P.P.,Dauter, Z.
Human Suv3 protein reveals unique features among SF2 helicases.
Acta Crystallogr.,Sect.D, 67:988-996, 2011

PubMed Abstract: Suv3 is a helicase that is involved in efficient turnover and surveillance of RNA in eukaryotes. In vitro studies show that human Suv3 (hSuv3) in complex with human polynucleotide phosphorylase has RNA degradosome activity. The enzyme is mainly localized in mitochondria, but small fractions are found in cell nuclei. Here, two X-ray crystallographic structures of human Suv3 in complex with AMPPNP, a nonhydrolysable analog of ATP, and with a short five-nucleotide strand of RNA are presented at resolutions of 2.08 and 2.9 Å, respectively. The structure of the enzyme is very similar in the two complexes and consists of four domains. Two RecA-like domains form the tandem typical of all helicases from the SF2 superfamily which together with the C-terminal all-helical domain makes a ring structure through which the nucleotide strand threads. The mostly helical N-terminal domain is positioned externally with respect to the core of the enzyme. Most of the typical helicase motifs are present in hSuv3, but the protein shows certain unique characteristics, suggesting that Suv3 enzymes may constitute a separate subfamily of helicases.

PubMed: 22101826
DOI: 10.1107/S0907444911040248

実験手法

X-RAY DIFFRACTION (2.9 Å)