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TitleCrystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism
Journal, issue, pagesJ. Biol. Chem., Vol. 277, Page 9512-9519, Year 2002
Publish dateDec 18, 2001 (structure data deposition date)
AuthorsPaetzel, M. / Dalbey, R.E. / Strynadka, N.C.J.
External linksJ. Biol. Chem. / PubMed:11741964
MethodsX-ray diffraction
Resolution2.4 Å
Structure data

PDB-1kn9:
CRYSTAL STRUCTURE OF A BACTERIAL SIGNAL PEPTIDASE APO-ENZYME, IMPLICATIONS FOR SIGNAL PEPTIDE BINDING AND THE SER-LYS DYAD MECHANISM.
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • escherichia coli k12 (bacteria)
KeywordsHYDROLASE / serine protease / Lysine general base / membrane protein / mostly beta-fold

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