4J94
Crystal structure of MycP1 from the ESX-1 type VII secretion system
Summary for 4J94
| Entry DOI | 10.2210/pdb4j94/pdb |
| Descriptor | Membrane-anchored mycosin mycp1 (2 entities in total) |
| Functional Keywords | subtilisin-like, protease, secretion system, hydrolase |
| Biological source | Mycobacterium smegmatis |
| Total number of polymer chains | 1 |
| Total formula weight | 42618.31 |
| Authors | Solomonson, M.,Wasney, G.A.,Watanabe, N.,Gruninger, R.J.,Prehna, G.,Strynadka, N.C.J. (deposition date: 2013-02-15, release date: 2013-05-01, Last modification date: 2024-11-06) |
| Primary citation | Solomonson, M.,Huesgen, P.F.,Wasney, G.A.,Watanabe, N.,Gruninger, R.J.,Prehna, G.,Overall, C.M.,Strynadka, N.C. Structure of the Mycosin-1 Protease from the Mycobacterial ESX-1 Protein Type VII Secretion System. J.Biol.Chem., 288:17782-17790, 2013 Cited by PubMed Abstract: Mycobacteria use specialized type VII (ESX) secretion systems to export proteins across their complex cell walls. Mycobacterium tuberculosis encodes five nonredundant ESX secretion systems, with ESX-1 being particularly important to disease progression. All ESX loci encode extracellular membrane-bound proteases called mycosins (MycP) that are essential to secretion and have been shown to be involved in processing of type VII-exported proteins. Here, we report the first x-ray crystallographic structure of MycP1(24-407) to 1.86 Å, defining a subtilisin-like fold with a unique N-terminal extension previously proposed to function as a propeptide for regulation of enzyme activity. The structure reveals that this N-terminal extension shows no structural similarity to previously characterized protease propeptides and instead wraps intimately around the catalytic domain where, tethered by a disulfide bond, it forms additional interactions with a unique extended loop that protrudes from the catalytic core. We also show MycP1 cleaves the ESX-1 secreted protein EspB from both M. tuberculosis and Mycobacterium smegmatis at a homologous cut site in vitro. PubMed: 23620593DOI: 10.1074/jbc.M113.462036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.857 Å) |
Structure validation
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