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Structure paper

TitleStructure-based mechanism of cysteine-switch latency and of catalysis by pappalysin-family metallopeptidases.
Journal, issue, pagesIucrj, Vol. 7, Page 18-29, Year 2020
Publish dateMar 29, 2019 (structure data deposition date)
AuthorsGuevara, T. / Rodriguez-Banqueri, A. / Ksiazek, M. / Potempa, J. / Gomis-Ruth, F.X.
External linksIucrj / PubMed:31949901
MethodsX-ray diffraction
Resolution1.4 - 1.6 Å
Structure data

PDB-6r7u:
Selenomethionine variant of Tannerella forsythia promirolysin mutant E225A
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-6r7v:
Tannerella forsythia promirolysin mutant E225A
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-6r7w:
Tannerella forsythia mature mirolysin in complex with a cleaved peptide.
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-BO3:
BORIC ACID

ChemComp-HOH:
WATER

ChemComp-EOH:
ETHANOL

ChemComp-CIT:
CITRIC ACID

Source
  • tannerella forsythia (bacteria)
  • tannerella forsythia (strain atcc 43037 / jcm 10827 / fdc 338) (bacteria)
KeywordsHYDROLASE / metallopeptidase zymogen / metzincin / pappalysin family / Tannerella forsythia / periodontopathogen / peridontal disease / periodontal disease

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