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Structure paper

TitleMolecular Characterization of a Novel Lytic Enzyme LysC from Clostridium intestinale URNW and Its Antibacterial Activity Mediated by Positively Charged N -Terminal Extension.
Journal, issue, pagesInt J Mol Sci, Vol. 21, Year 2020
Publish dateSep 6, 2019 (structure data deposition date)
AuthorsPlotka, M. / Szadkowska, M. / Hakansson, M. / Kovacic, R. / Al-Karadaghi, S. / Walse, B. / Werbowy, O. / Kaczorowska, A.K. / Kaczorowski, T.
External linksInt J Mol Sci / PubMed:32664473
MethodsX-ray diffraction
Resolution1.2 - 1.21 Å
Structure data

PDB-6ssc:
N-acetylmuramoyl-L-alanine amidase LysC from Clostridium intestinale URNW
Method: X-RAY DIFFRACTION / Resolution: 1.21 Å

PDB-6su5:
Ph2119 endolysin from Thermus scotoductus MAT2119 bacteriophage Ph2119
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • clostridium intestinale (bacteria)
  • thermus phage 2119 (virus)
KeywordsHYDROLASE / amidase / zinc binding / cell wall degradation / endolysine

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