Ontology highlight
ABSTRACT:
SUBMITTER: Rasmussen KK
PROVIDER: S-EPMC4941734 | biostudies-literature | 2016 Jul
REPOSITORIES: biostudies-literature
Rasmussen Kim Krighaar KK Frandsen Kristian E H KE Boeri Erba Elisabetta E Pedersen Margit M Varming Anders K AK Hammer Karin K Kilstrup Mogens M Thulstrup Peter W PW Blackledge Martin M Jensen Malene Ringkjøbing MR Lo Leggio Leila L
Scientific reports 20160712
The CI repressor from the temperate bacteriophage TP901-1 consists of two folded domains, an N-terminal helix-turn-helix DNA-binding domain (NTD) and a C-terminal oligomerization domain (CTD), which we here suggest to be further divided into CTD1 and CTD2. Full-length CI is a hexameric protein, whereas a truncated version, CI∆58, forms dimers. We identify the dimerization region of CI∆58 as CTD1 and determine its secondary structure to be helical both within the context of CI∆58 and in isolation ...[more]