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TitleFunctional analysis ofClostridium difficilesortase B reveals key residues for catalytic activity and substrate specificity.
Journal, issue, pagesJ. Biol. Chem., Vol. 295, Page 3734-3745, Year 2020
Publish dateSep 17, 2019 (structure data deposition date)
AuthorsKang, C.Y. / Huang, I.H. / Chou, C.C. / Wu, T.Y. / Chang, J.C. / Hsiao, Y.Y. / Cheng, C.H. / Tsai, W.J. / Hsu, K.C. / Wang, S.
External linksJ. Biol. Chem. / PubMed:32005667
MethodsX-ray diffraction
Resolution2.604 - 3.1 Å
Structure data

PDB-6kyc:
Structure of the S207A mutant of Clostridium difficile sortase B
Method: X-RAY DIFFRACTION / Resolution: 2.604 Å

PDB-6kyd:
Structure of the R217A mutant of Clostridium difficile sortase B
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • peptoclostridium difficile 630 (bacteria)
  • clostridioides difficile 630 (bacteria)
KeywordsHYDROLASE / sortase B / cysteine transpeptidase / Clostridium difficile

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