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Structure paper

TitleHigh avidity drives the interaction between the streptococcal C1 phage endolysin, PlyC, with the cell surface carbohydrates of Group A Streptococcus.
Journal, issue, pagesMol. Microbiol., Vol. 116, Page 397-415, Year 2021
Publish dateDec 2, 2020 (structure data deposition date)
AuthorsBroendum, 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 linksMol. Microbiol. / PubMed:33756056
MethodsX-ray diffraction
Resolution1.7 - 1.8 Å
Structure data

PDB-7kwt:
X-ray Crystal Structure of PlyCB Mutant Y28H
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

PDB-7kww:
X-ray Crystal Structure of PlyCB Mutant K59H
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-7kwy:
X-ray Crystal Structure of PlyCB Mutant R66K
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

Source
  • streptococcus virus c1
KeywordsANTIMICROBIAL PROTEIN / ENDOLYSIN / VIRAL PROTEIN / PHAGE EFFECTOR PROTEIN

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