4F88

X-ray Crystal Structure of PlyC

Summary for 4F88

• Entry DOI: 10.2210/pdb4f88/pdb
• Related: 4F87
• Descriptor: PlyCA, PlyCB (2 entities in total)
• Functional Keywords: lysin, bacteriophage, antimicrobial protein, viral protein
• Biological source: Streptococcus phage C1; More
• Total number of polymer chains: 18
• Total formula weight: 229040.09

Authors

McGowan, S.,Buckle, A.M.,Fischetti, V.A.,Nelson, D.C.,Whisstock, J.C. (deposition date: 2012-05-17, release date: 2012-07-25, Last modification date: 2023-09-13)

Primary citation

McGowan, S.,Buckle, A.M.,Mitchell, M.S.,Hoopes, J.T.,Gallagher, D.T.,Heselpoth, R.D.,Shen, Y.,Reboul, C.F.,Law, R.H.,Fischetti, V.A.,Whisstock, J.C.,Nelson, D.C.
X-ray crystal structure of the streptococcal specific phage lysin PlyC.
Proc.Natl.Acad.Sci.USA, 109:12752-12757, 2012

PubMed Abstract: Bacteriophages deploy lysins that degrade the bacterial cell wall and facilitate virus egress from the host. When applied exogenously, these enzymes destroy susceptible microbes and, accordingly, have potential as therapeutic agents. The most potent lysin identified to date is PlyC, an enzyme assembled from two components (PlyCA and PlyCB) that is specific for streptococcal species. Here the structure of the PlyC holoenzyme reveals that a single PlyCA moiety is tethered to a ring-shaped assembly of eight PlyCB molecules. Structure-guided mutagenesis reveals that the bacterial cell wall binding is achieved through a cleft on PlyCB. Unexpectedly, our structural data reveal that PlyCA contains a glycoside hydrolase domain in addition to the previously recognized cysteine, histidine-dependent amidohydrolases/peptidases catalytic domain. The presence of eight cell wall-binding domains together with two catalytic domains may explain the extraordinary potency of the PlyC holoenyzme toward target bacteria.

PubMed: 22807482
DOI: 10.1073/pnas.1208424109

Experimental method

X-RAY DIFFRACTION (3.3 Å)