Data from computational analysis of the peptide linkers in the MocR bacterial transcriptional regulators
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...
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doaj-f2998992d88343f8bcf5ac1e78b3cffe2020-11-25T00:08:53ZengElsevierData in Brief2352-34092016-12-019C29231310.1016/j.dib.2016.08.064Data from computational analysis of the peptide linkers in the MocR bacterial transcriptional regulatorsSebastiana Angelaccio0Teresa Milano1Angela Tramonti2Martino Luigi Di Salvo3Roberto Contestabile4Stefano Pascarella5Dipartimento di Scienze biochimiche “A. Rossi Fanelli”, Sapienza Università di Roma, 00185 Roma, ItalyDipartimento di Scienze biochimiche “A. Rossi Fanelli”, Sapienza Università di Roma, 00185 Roma, ItalyIstituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, 00185 Roma, ItalyDipartimento di Scienze biochimiche “A. Rossi Fanelli”, Sapienza Università di Roma, 00185 Roma, ItalyDipartimento di Scienze biochimiche “A. Rossi Fanelli”, Sapienza Università di Roma, 00185 Roma, ItalyDipartimento di Scienze biochimiche “A. Rossi Fanelli”, Sapienza Università di Roma, 00185 Roma, ItalyDetailed 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].http://www.sciencedirect.com/science/article/pii/S2352340916305650Linker peptideLinker lengthMocR regulatorsLinker engineeringPdxRGabRHydrophobicityFlexibilityResidue propensityDyad propensity |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Sebastiana Angelaccio Teresa Milano Angela Tramonti Martino Luigi Di Salvo Roberto Contestabile Stefano Pascarella |
spellingShingle |
Sebastiana Angelaccio Teresa Milano Angela Tramonti Martino Luigi Di Salvo Roberto Contestabile Stefano Pascarella Data from computational analysis of the peptide linkers in the MocR bacterial transcriptional regulators Data in Brief Linker peptide Linker length MocR regulators Linker engineering PdxR GabR Hydrophobicity Flexibility Residue propensity Dyad propensity |
author_facet |
Sebastiana Angelaccio Teresa Milano Angela Tramonti Martino Luigi Di Salvo Roberto Contestabile Stefano Pascarella |
author_sort |
Sebastiana Angelaccio |
title |
Data from computational analysis of the peptide linkers in the MocR bacterial transcriptional regulators |
title_short |
Data from computational analysis of the peptide linkers in the MocR bacterial transcriptional regulators |
title_full |
Data from computational analysis of the peptide linkers in the MocR bacterial transcriptional regulators |
title_fullStr |
Data from computational analysis of the peptide linkers in the MocR bacterial transcriptional regulators |
title_full_unstemmed |
Data from computational analysis of the peptide linkers in the MocR bacterial transcriptional regulators |
title_sort |
data from computational analysis of the peptide linkers in the mocr bacterial transcriptional regulators |
publisher |
Elsevier |
series |
Data in Brief |
issn |
2352-3409 |
publishDate |
2016-12-01 |
description |
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]. |
topic |
Linker peptide Linker length MocR regulators Linker engineering PdxR GabR Hydrophobicity Flexibility Residue propensity Dyad propensity |
url |
http://www.sciencedirect.com/science/article/pii/S2352340916305650 |
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