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Structure paper

TitleStaphylococcal SplB Serine Protease Utilizes a Novel Molecular Mechanism of Activation.
Journal, issue, pagesJ. Biol. Chem., Vol. 289, Page 15544-15553, Year 2014
Publish dateApr 5, 2013 (structure data deposition date)
AuthorsPustelny, K. / Zdzalik, M. / Stach, N. / Stec-Niemczyk, J. / Cichon, P. / Czarna, A. / Popowicz, G. / Mak, P. / Drag, M. / Salvesen, G.S. ...Pustelny, K. / Zdzalik, M. / Stach, N. / Stec-Niemczyk, J. / Cichon, P. / Czarna, A. / Popowicz, G. / Mak, P. / Drag, M. / Salvesen, G.S. / Wladyka, B. / Potempa, J. / Dubin, A. / Dubin, G.
External linksJ. Biol. Chem. / PubMed:24713703
MethodsX-ray diffraction
Resolution1.6 - 1.96 Å
Structure data

PDB-4k1s:
Gly-Ser-SplB protease from Staphylococcus aureus at 1.96 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.96 Å

PDB-4k1t:
Gly-Ser-SplB protease from Staphylococcus aureus at 1.60 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

Source
  • staphylococcus aureus (bacteria)
KeywordsHYDROLASE / chymotrypsin-like fold / serine protease / extracellular

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