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B6db references: 26026720

type Journal Article
authors Milano T, Contestabile R, Lo Presti A, Ciccozzi M, Pascarella S
title The aspartate aminotransferase-like domain of Firmicutes MocR transcriptional regulators
journal Comput Biol Chem
Activity mocr
sel selected
ui 26026720
year (2015)
volume 58
pages 55-61
keywords Bacterial transcriptional regulation; Bioinformatics; Evolution; Fold type-I; MocR; Pyridoxal-5′-phosphate
abstract Bacterial MocR transcriptional regulators possess an N-terminal DNA-binding domain containing a conserved helix-turn-helix module and an effector-binding and/or oligomerization domain at the C-terminus, homologous to fold type-I pyridoxal 5'-phosphate (PLP) enzymes. Since a comprehensive structural analysis of the MocR regulators is still missing, a comparisons of Firmicutes MocR sequences was undertook to contribute to the understanding of the structural characteristics of the C-terminal domain of these proteins, and to shed light on the structural and functional relationship with fold type-I PLP enzymes. Results of this work suggest the presence of at least three subgroups within the MocR sequences and provide a guide for rational site-directed mutagenesis studies aimed at deciphering the structure-function relationships in this new protein family.
last changed 2017/10/26 14:33

B6db references