6TFL

Lsm protein (SmAP) from Halobacterium salinarum

6TFL の概要

• エントリーDOI: 10.2210/pdb6tfl/pdb
• 関連するPDBエントリー: 1LJO
• 分子名称: RNA-binding protein Lsm, CALCIUM ION, URIDINE, ... (5 entities in total)
• 機能のキーワード: lsm, smap, rna-chaperon, rna binding protein
• 由来する生物種: Halobacterium salinarum R1
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 99378.34

構造登録者

Nikulin, A.D.,Fando, M.S.,Lekontseva, N.V. (登録日: 2019-11-14, 公開日: 2020-11-25, 最終更新日: 2024-01-24)

主引用文献

Fando, M.S.,Mikhaylina, A.O.,Lekontseva, N.V.,Tishchenko, S.V.,Nikulin, A.D.
Structure and RNA-Binding Properties of Lsm Protein from Halobacterium salinarum.
Biochemistry Mosc., 86:833-842, 2021

PubMed Abstract: The structure and the RNA-binding properties of the Lsm protein from Halobacterium salinarum have been determined. A distinctive feature of this protein is the presence of a short L4 loop connecting the β3 and β4 strands. Since bacterial Lsm proteins (also called Hfq proteins) have a short L4 loop and form hexamers, whereas archaeal Lsm proteins (SmAP) have a long L4 loop and form heptamers, it has been suggested that the length of the L4 loop may affect the quaternary structure of Lsm proteins. Moreover, the L4 loop covers the region of SmAP corresponding to one of the RNA-binding sites in Hfq, and thus can affect the RNA-binding properties of the protein. Our results show that the SmAP from H. salinarum forms heptamers and possesses the same RNA-binding properties as homologous proteins with the long L4 loop. Therefore, the length of the L4 does not govern the number of monomers in the protein particles and does not affect the RNA-binding properties of Lsm proteins.

PubMed: 34284708
DOI: 10.1134/S000629792107004X

実験手法

X-RAY DIFFRACTION (2.397 Å)