4kpg

Crystal structure of MycP1 from the ESX-1 type VII secretion system

spinqualitylabelsall models 4kpg, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4kpg is a 1 chain structure with sequence from Mycolicibacterium smegmatis MC2 155. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.148Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MYCP1_MYCS2 May play a dual role in regulation of ESX-1 secretion and virulence. Acts as a protease that cleaves EspB. Publication Abstract from PubMed 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 A, 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. Structure of the Mycosin-1 Protease from the Mycobacterial ESX-1 Protein Type VII Secretion System.,Solomonson M, Huesgen PF, Wasney GA, Watanabe N, Gruninger RJ, Prehna G, Overall CM, Strynadka NC J Biol Chem. 2013 Jun 14;288(24):17782-90. doi: 10.1074/jbc.M113.462036. Epub, 2013 Apr 25. PMID:23620593 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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