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Structure paper

TitleRole of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins.
Journal, issue, pagesJ. Biol. Chem., Vol. 286, Page 34391-34403, Year 2011
Publish dateMay 29, 2009 (structure data deposition date)
AuthorsLow, L.Y. / Yang, C. / Perego, M. / Osterman, A. / Liddington, R.
External linksJ. Biol. Chem. / PubMed:21816821
MethodsX-ray diffraction
Resolution1.44 - 2.7 Å
Structure data

PDB-3hmb:
Mutant endolysin from Bacillus subtilis
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-3hmc:
Endolysin from Bacillus anthracis
Method: X-RAY DIFFRACTION / Resolution: 1.44 Å

PDB-3rdr:
Structure of the catalytic domain of XlyA
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-CL:
Unknown entry

Source
  • bacillus subtilis (bacteria)
  • bacillus anthracis (anthrax bacterium)
KeywordsHYDROLASE / endolysin / amidase / Cell wall biogenesis/degradation / Competence / Secreted / Sporulation / glycosyl hydrolase / T7 lysozyme fold

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