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Title | High avidity drives the interaction between the streptococcal C1 phage endolysin, PlyC, with the cell surface carbohydrates of Group A Streptococcus. |
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Journal, issue, pages | Mol. Microbiol., Vol. 116, Page 397-415, Year 2021 |
Publish date | Dec 2, 2020 (structure data deposition date) |
Authors | Broendum, S.S. / Williams, D.E. / Hayes, B.K. / Kraus, F. / Fodor, J. / Clifton, B.E. / Geert Volbeda, A. / Codee, J.D.C. / Riley, B.T. / Drinkwater, N. ...Broendum, S.S. / Williams, D.E. / Hayes, B.K. / Kraus, F. / Fodor, J. / Clifton, B.E. / Geert Volbeda, A. / Codee, J.D.C. / Riley, B.T. / Drinkwater, N. / Farrow, K.A. / Tsyganov, K. / Heselpoth, R.D. / Nelson, D.C. / Jackson, C.J. / Buckle, A.M. / McGowan, S. |
External links | Mol. Microbiol. / PubMed:33756056 |
Methods | X-ray diffraction |
Resolution | 1.7 - 1.8 Å |
Structure data | PDB-7kwt: PDB-7kww: PDB-7kwy: |
Chemicals | ChemComp-HOH: ChemComp-MPD: |
Source |
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Keywords | ANTIMICROBIAL PROTEIN / ENDOLYSIN / VIRAL PROTEIN / PHAGE EFFECTOR PROTEIN |