|
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 |
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