5a6s

Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product

spinqualitylabelsall models 5a6s, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a6s is a 2 chain structure with sequence from Clostridium phage phiCTP1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: 1PE, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D9ZNF3_9CAUD Publication Abstract from PubMed Bacteriophages produce endolysins, which lyse the bacterial host cell to release newly produced virions. The timing of lysis is regulated, and is thought to involve the activation of a molecular switch. We present a crystal structure of the activated endolysin CTP1L that targets Clostridium tyrobutyricum, consisting of a complex between the full length protein and an N-terminally truncated C-terminal cell wall binding domain (CBD). The truncated CBD is produced through an internal translation start site within the endolysin gene. Mutants affecting the internal translation site change the oligomeric state of the endolysin, and reduce lytic activity. The activity can be modulated by reconstitution of the full length endolysin-CBD complex with free CBD. The same oligomerization mechanism applies to the CD27L endolysin that targets Clostridium difficile and the CS74L endolysin that targets Clostridium sporogenes. When the CTP1L endolysin gene is introduced into the commensal bacterium Lactococcus lactis, the truncated CBD is also produced, showing that the alternative start codon can be used in other bacterial species. The identification of a translational switch affecting oligomerization presented here has implications for the design of effective endolysins for the treatment of bacterial infections. Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product.,Dunne M, Leicht S, Krichel B, Mertens HD, Thompson A, Krijgsveld J, Svergun DI, Gomez-Torres N, Garde S, Uetrecht C, Narbad A, Mayer MJ, Meijers R J Biol Chem. 2015 Dec 18. pii: jbc.M115.671172. PMID:26683375 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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