Ontology highlight
ABSTRACT:
SUBMITTER: Angelaccio S
PROVIDER: S-EPMC5026710 | biostudies-literature | 2016 Dec
REPOSITORIES: biostudies-literature
Angelaccio Sebastiana S Milano Teresa T Tramonti Angela A Di Salvo Martino Luigi ML Contestabile Roberto R Pascarella Stefano S
Data in brief 20160905
Detailed data from statistical analyses of the structural properties of the inter-domain linker peptides of the bacterial regulators of the family MocR are herein reported. MocR regulators are a recently discovered subfamily of bacterial regulators possessing an N-terminal domain, 60 residue long on average, folded as the winged-helix-turn-helix architecture responsible for DNA recognition and binding, and a large C-terminal domain (350 residue on average) that belongs to the fold type-I pyridox ...[more]