4f88 | pdb_00004f88

X-ray Crystal Structure of PlyC

spinqualitylabelsall models 4f88, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4f88 is a 18 chain structure with sequence from Streptococcus phage c1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4f87 Gene: orf11 (Streptococcus phage C1), orf9 (Streptococcus phage C1) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. X-ray crystal structure of the streptococcal specific phage lysin PlyC.,McGowan S, Buckle AM, Mitchell MS, Hoopes JT, Gallagher DT, Heselpoth RD, Shen Y, Reboul CF, Law RH, Fischetti VA, Whisstock JC, Nelson DC Proc Natl Acad Sci U S A. 2012 Jul 17. PMID:22807482 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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