Article
Crystal Structure of the CTP1L Endolysin Reveals How Its Activity Is Regulated by a Secondary Translation Product.
The Journal of biological chemistry - 4 Mar 2016
Dunne Matthew, Leicht Stefan, Krichel Boris, Mertens Haydyn D T, Thompson Andrew, Krijgsveld Jeroen, Svergun Dmitri I, Gómez-Torres Natalia, Garde Sonia, Uetrecht Charlotte, Narbad Arjan, Mayer Melinda J, Meijers Rob
Abstract excerpt
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...
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