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TitleCrystal Structure of the CTP1L Endolysin Reveals How Its Activity Is Regulated by a Secondary Translation Product.
Journal, issue, pagesJ Biol Chem, Vol. 291, Issue 10, Page 4882-4893, Year 2016
Publish dateMar 4, 2016
AuthorsMatthew Dunne / Stefan Leicht / Boris Krichel / Haydyn D T Mertens / Andrew Thompson / Jeroen Krijgsveld / Dmitri I Svergun / Natalia Gómez-Torres / Sonia Garde / Charlotte Uetrecht / Arjan Narbad / Melinda J Mayer / Rob Meijers /
PubMed AbstractBacteriophages 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 ...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.
External linksJ Biol Chem / PubMed:26683375 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution1.9 Å
Structure data

SASDAD7:
Structure of a complex between full length and truncated CTP1L endolysin
Method: SAXS/SANS

SASDAE7:
Structure of a complex between full length and truncated CS74L endolysin
Method: SAXS/SANS

PDB-5a6s:
Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM / Polyethylene glycol

ChemComp-HOH:
WATER / Water

Source
  • clostridium phage phictp1 (virus)
  • Clostridium phage phi8074-b1 (virus)
KeywordsSTRUCTURAL PROTEIN / ENDOLYSIN / SECONDARY TRANSLATION PRODUCT / BACTERIOPHAGE

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