5A6S

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

5A6S の概要

• エントリーDOI: 10.2210/pdb5a6s/pdb
• 分子名称: ENDOLYSIN, SULFATE ION, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: structural protein, endolysin, secondary translation product, bacteriophage
• 由来する生物種: CLOSTRIDIUM PHAGE PHICTP1; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42518.92

構造登録者

Dunne, M.,Leicht, S.,Krichel, B.,Mertens, H.D.T.,Thompson, A.,Krijgsveld, J.,Svergun, D.I.,GomezTorres, N.,Garde, S.,Uetrecht, C.,Narbad, A.,Mayer, M.J.,Meijers, R. (登録日: 2015-07-01, 公開日: 2015-12-30, 最終更新日: 2024-01-10)

主引用文献

Dunne, M.,Leicht, S.,Krichel, B.,Mertens, H.D.T.,Thompson, A.,Krijgsveld, J.,Svergun, D.I.,Gomez-Torres, N.,Garde, S.,Uetrecht, C.,Narbad, A.,Mayer, M.J.,Meijers, R.
Crystal Structure of the Ctp1L Endolysin Reveals How its Activity is Regulated by a Secondary Translation Product.
J.Biol.Chem., 291:4882-, 2016

PubMed Abstract: 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.

PubMed: 26683375
DOI: 10.1074/JBC.M115.671172

実験手法

X-RAY DIFFRACTION (1.9 Å)