title: The aspartate aminotransferase-like domain of Firmicutes MocR transcriptional regulators.
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.
authors.affiliation: Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università La Sapienza, 00185 Roma, Italy.
authors.forename: Teresa
authors.initials: T
authors.lastname: Milano
authors.affiliation: Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università La Sapienza, 00185 Roma, Italy.
authors.forename: Roberto
authors.initials: R
authors.lastname: Contestabile
authors.affiliation: Dipartimento di Malattie Infettive, Parassitarie e Immunomediate, Istituto Superiore di Sanità, 00185 Roma, Italy.
authors.forename: Alessandra
authors.initials: A
authors.lastname: Lo Presti
authors.affiliation: Dipartimento di Malattie Infettive, Parassitarie e Immunomediate, Istituto Superiore di Sanità, 00185 Roma, Italy.
authors.forename: Massimo
authors.initials: M
authors.lastname: Ciccozzi
authors.affiliation: Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università La Sapienza, 00185 Roma, Italy. Electronic address: Stefano.Pascarella@uniroma1.it.
authors.forename: Stefano
authors.initials: S
authors.lastname: Pascarella
mesh_terms: D001219:Aspartate Aminotransferases; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D001483:Base Sequence; D000068536:Bacillota / Q000235:genetics; D010802:Phylogeny; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017385:Sequence Homology; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics; D014158:Transcription, Genetic
chemical_list: D001426:Bacterial Proteins; D014157:Transcription Factors; D001219:Aspartate Aminotransferases
keywords: Bacterial transcriptional regulation; Bioinformatics; Evolution; Fold type-I; MocR; Pyridoxal-5′-phosphate