Data from computational analysis of the peptide linkers in the MocR bacterial transcriptional regulators

• Main Authors: Sebastiana Angelaccio, Teresa Milano, Angela Tramonti, Martino Luigi Di Salvo, Roberto Contestabile, Stefano Pascarella
• Format: Article
• Language: English
• Published: Elsevier 2016-12-01
• Series: Data in Brief
• Subjects: Linker peptide; Linker length; MocR regulators; Linker engineering; PdxR; GabR; Hydrophobicity; Flexibility; Residue propensity; Dyad propensity
• Online Access: http://www.sciencedirect.com/science/article/pii/S2352340916305650

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 pyridoxal 5′-phosphate (PLP) dependent enzymes such aspartate aminotransferase. Data show the distribution of several structural characteristics of the linkers taken from bacterial species from five different phyla, namely Actinobacteria, Alpha-, Beta-, Gammaproteobacteria and Firmicutes. Interpretation and discussion of reported data refer to the article “Structural properties of the linkers connecting the N- and C- terminal domains in the MocR bacterial transcriptional regulators” (T. Milano, S. Angelaccio, A. Tramonti, M. L. Di Salvo, R. Contestabile, S. Pascarella, 2016) [1].