8VJM
SpoIVFB(E44Q variant):pro-sigmaK complex
Summary for 8VJM
| Entry DOI | 10.2210/pdb8vjm/pdb |
| Related | 8VJL |
| EMDB information | 43288 43289 |
| Descriptor | Stage IV sporulation protein FB, RNA polymerase sigma-K factor, Lauryl Maltose Neopentyl Glycol, ... (4 entities in total) |
| Functional Keywords | spoivfb, sigmak, s2p, site-2-protease, protease, membrane protein |
| Biological source | Bacillus subtilis subsp. subtilis str. 168 More |
| Total number of polymer chains | 4 |
| Total formula weight | 106862.45 |
| Authors | Orlando, M.A.,Pouillon, H.J.T.,Mandal, S.,Kroos, L.,Orlando, B.J. (deposition date: 2024-01-07, release date: 2024-10-02, Last modification date: 2024-10-30) |
| Primary citation | Orlando, M.A.,Pouillon, H.J.T.,Mandal, S.,Kroos, L.,Orlando, B.J. Substrate engagement by the intramembrane metalloprotease SpoIVFB. Nat Commun, 15:8276-8276, 2024 Cited by PubMed Abstract: S2P intramembrane metalloproteases regulate diverse signaling pathways across all three domains of life. However, the mechanism by which S2P metalloproteases engage substrates and catalyze peptide hydrolysis within lipid membranes has remained elusive. Here we determine the cryo-EM structure of the S2P family intramembrane metalloprotease SpoIVFB from Bacillus subtilis bound to its native substrate Pro-σ. The structure and accompanying biochemical data demonstrate that SpoIVFB positions Pro-σ at the enzyme active site through a β-sheet augmentation mechanism, and reveal key interactions between Pro-σ and the interdomain linker connecting SpoIVFB transmembrane and CBS domains. The cryo-EM structure and molecular dynamics simulation reveal a plausible path for water to access the membrane-buried active site of SpoIVFB, and suggest a possible role of membrane lipids in facilitating substrate capture. These results provide key insight into how S2P intramembrane metalloproteases capture and position substrates for hydrolytic proteolysis within the hydrophobic interior of a lipid membrane. PubMed: 39419996DOI: 10.1038/s41467-024-52634-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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