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Título

Predicted structure and function of FADS-type II protein from Listeria monocytogenes.

AutorYruela Guerrero, Inmaculada ; Ferreira, Patricia ; Martínez-Júlvez, Marta; Contreras-Moreira, Bruno ; Medina, Milagros
Fecha de publicación23-ene-2014
CitaciónVI International Conference BIFI 2014. Exploring the role of computation in Science: from Biology to Physics (22-24.01.2014, Zaragoza, Spain)
ResumenFlavin adenine dinucleotide synthetases (FADSs) are known as a group of prokaryotic bifunctional enzymes that carry out the dual functions of riboflavin phosphorylation to produce flavin mononucleotide (FMN) and its subsequent adenylylation to generate FAD (hereafter FADS-type 1). A recent work [1] using a variety of bioinformatics methods revealed that certain gram-positive pathogenic bacteria (i.e. Listeria monocytonegens, Listeria welshimeri, Lactobacillus plan tarum, Bacillus cytotoxicus) contain also a variant of FADS sequences, named FADS-type II. These two types of sequences cluster together. Although the phylogenetic tree does not support that FADStype II proteins constitute a distinct evolutionary class, their shorter and non-conserved C-terminal domains suggest them as a distinct functional group unable to produce riboflavin phosphorylation. In this work the putative structure and function of the Cterminal domain of the FADS-type II from Listeria monocytonegens (LmFADS-typell) has been investigated. The results point out that this C-terminal domain contains a LPAxGxY conserved sequence motif with high homology with the LPASGxY consensus sequence common to proteins acting as lysozyme inhibitors, such as P1iG, P1iC and Plil, in gram-negative bacteria. This motif has been shown to be important for lysozyme inhibition in the P1iC and Plil families, defending bacteria against the lytic action of host lysozymes [2]. In gram-positive bacteria no homology was found with lysozyme inhibitors. Interestingly, in this bacterium linage homologies were found with FMN reductases domains. A structural model for the C-terminal domain of LmFADStype II is also proposed.
URIhttp://hdl.handle.net/10261/127430
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