6F9M

The LIPY/F-motif in an intracellular subtilisin protease is involved in inhibition

6F9M の概要

• エントリーDOI: 10.2210/pdb6f9m/pdb
• 分子名称: Serine protease, TRIETHYLENE GLYCOL, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: isp, lipy/f-motif, subtilisin, protease structure, hydrolase
• 由来する生物種: Planococcus plakortidis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71613.56

構造登録者

Bjerga, G.E.K.,Larsen, O.,Arsin, H.,Williamson, A.K.,Garcia-Moyano, A.,Leiros, I.,Puntervoll, P. (登録日: 2017-12-14, 公開日: 2018-06-27, 最終更新日: 2024-01-17)

主引用文献

Bjerga, G.E.K.,Larsen, O.,Williamson, A.,Garcia-Moyano, A.,Leiros, I.,Puntervoll, P.
Mutational analysis of the pro-peptide of a marine intracellular subtilisin protease supports its role in inhibition.
Proteins, 86:965-977, 2018

PubMed Abstract: Intracellular subtilisin proteases (ISPs) have important roles in protein processing during the stationary phase in bacteria. Their unregulated protein degrading activity may have adverse effects inside a cell, but little is known about their regulatory mechanism. Until now, ISPs have mostly been described from Bacillus species, with structural data from a single homolog. Here, we study a marine ISP originating from a phylogenetically distinct genus, Planococcus sp. The enzyme was successfully overexpressed in E. coli, and is active in presence of calcium, which is thought to have a role in minor, but essential, structural rearrangements needed for catalytic activity. The ISP operates at alkaline pH and at moderate temperatures, and has a corresponding melting temperature around 60 °C. The high-resolution 3-dimensional structure reported here, represents an ISP with an intact catalytic triad albeit in a configuration with an inhibitory pro-peptide bound. The pro-peptide is removed in other homologs, but the removal of the pro-peptide from the Planococcus sp. AW02J18 ISP appears to be different, and possibly involves several steps. A first processing step is described here as the removal of 2 immediate N-terminal residues. Furthermore, the pro-peptide contains a conserved LIPY/F-motif, which was found to be involved in inhibition of the catalytic activity.

PubMed: 29907987
DOI: 10.1002/prot.25528

実験手法

X-RAY DIFFRACTION (1.298 Å)