4m1z

Crystal structure of MycP1 with the N-terminal propeptide removed

spinqualitylabelsall models 4m1z, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4m1z is a 4 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 2.25Å 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 Mycosin-1 protease (MycP1) is a serine protease anchored to the inner membrane of Mycobacterium tuberculosis, and is essential in virulence factor secretion through the ESX-1 type VII secretion system (T7SS). Bacterial physiology studies demonstrated that MycP1 plays a dual role in the regulation of ESX-1 secretion and virulence, primarily through cleavage of its secretion substrate EspB. MycP1 contains a putative N-terminal inhibitory propeptide and a catalytic triad of Asp-His-Ser, classic hallmarks of a subtilase family serine protease. The MycP1 propeptide was previously reported to be initially inactive and activated after prolonged incubation. In this study, we have determined crystal structures of MycP1 with (MycP1(2)(4)(-)(4)(2)(2)) and without (MycP1(6)(3)(-)(4)(2)(2)) the propeptide, and conducted EspB cleavage assays using the two proteins. Very high structural similarity was observed in the two crystal structures. Interestingly, protease assays demonstrated positive EspB cleavage for both proteins, indicating that the putative propeptide does not inhibit protease activity. Molecular dynamic simulations showed higher rigidity in regions guarding the entrance to the catalytic site in MycP1(2)(4)(-)(4)(2)(2) than in MycP1(6)(3)(-)(4)(2)(2), suggesting that the putative propeptide might contribute to the conformational stability of the active site cleft and surrounding regions. The putative propeptide of MycP1 in mycobacterial type VII secretion system does not inhibit protease activity but improves protein stability.,Sun D, Liu Q, He Y, Wang C, Wu F, Tian C, Zang J Protein Cell. 2013 Dec;4(12):921-31. doi: 10.1007/s13238-013-3089-7. Epub 2013, Nov 18. PMID:24248472 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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