Article open access publication

Structural basis of the bacteriophage TP901‐1 CI repressor dimerization and interaction with DNA

FEBS Letters, Wiley, ISSN 0014-5793

Volume 592, 10, 2018

DOI:10.1002/1873-3468.13060, Dimensions: pub.1103590484, PMID: 29683476,



  1. (1) University of Copenhagen, grid.5254.6, KU
  2. (2) French National Centre for Scientific Research, grid.4444.0







Temperate bacteriophages are known for their bistability, which in TP901-1 is controlled by two proteins, CI and MOR. Clear 1 repressor (CI) is hexameric and binds three palindromic operator sites via an N-terminal helix-turn-helix domain (NTD). A dimeric form, such as the truncated CI∆58 investigated here, is necessary for high-affinity binding to DNA. The crystal structure of the dimerization region (CTD1 ) is determined here, showing that it forms a pair of helical hooks. This newly determined structure is used together with the known crystal structure of the CI-NTD and small angle X-ray scattering data, to determine the solution structure of CI∆58 in complex with a palindromic operator site, showing that the two NTDs bind on opposing sides of the DNA helix.


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