6F9M
The LIPY/F-motif in an intracellular subtilisin protease is involved in inhibition
Summary for 6F9M
| Entry DOI | 10.2210/pdb6f9m/pdb |
| Descriptor | Serine protease, TRIETHYLENE GLYCOL, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | isp, lipy/f-motif, subtilisin, protease structure, hydrolase |
| Biological source | Planococcus plakortidis |
| Total number of polymer chains | 2 |
| Total formula weight | 71613.56 |
| Authors | Bjerga, G.E.K.,Larsen, O.,Arsin, H.,Williamson, A.K.,Garcia-Moyano, A.,Leiros, I.,Puntervoll, P. (deposition date: 2017-12-14, release date: 2018-06-27, Last modification date: 2024-01-17) |
| Primary citation | 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 Cited by 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: 29907987DOI: 10.1002/prot.25528 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.298 Å) |
Structure validation
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