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