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TitleThe putative propeptide of MycP1 in mycobacterial type VII secretion system does not inhibit protease activity but improves protein stability.
Journal, issue, pagesProtein Cell, Vol. 4, Page 921-931, Year 2013
Publish dateApr 23, 2013 (structure data deposition date)
AuthorsSun, D. / Liu, Q. / He, Y. / Wang, C. / Wu, F. / Tian, C. / Zang, J.
External linksProtein Cell / PubMed:24248472
MethodsX-ray diffraction
Resolution2.15 - 2.25 Å
Structure data

PDB-4kb5:
Crystal structure of MycP1 from Mycobacterium smegmatis
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-4m1z:
Crystal structure of MycP1 with the N-terminal propeptide removed
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • mycobacterium smegmatis (bacteria)
KeywordsHYDROLASE / subtilisin-like serine protease; subtilase family; catalytic triad; autoinhibition / Serine protease / subtilisin-like / propeptide-removed / ESX-1 system / membrane-anchored

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