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Revista Colombiana de Química
versión impresa ISSN 0120-2804versión On-line ISSN 2357-3791
Resumen
D-KERYND, Barona y DUVERNEY, Gaviria. In silico modeling of Pseudomonas fluoresceins organomercurial lyase (MerB). Rev.Colomb.Quim. [online]. 2022, vol.51, n.1, pp.14-23. Epub 26-Oct-2022. ISSN 0120-2804.
In silico modeling has made a great contribution to proteomic processes, developing structures of the already existing protein sequences, which for reasons of high costs and the different technologies necessary for the development of these methodologies, are deficient in the number of models of available proteins. Among those sequences lacking protein structure is the organomercurial lyase (MerB) protein from Pseudomonas fluoresceins, important in mercury resistance. In this article, the MerB protein in Pseudomonas fluorescens was analyzed both structurally and functionally, using the structural chemistry tool "homology modeling" using bioinformatic platforms, in order to obtain a model that represents the most accurate 3D structure and that captures the best structural variants among all the possible conformations of the proteins in the family. In this work, a comparative method of the sequence studied with those reported in the databases for MerB proteins of the genus Pseudomonas was developed. A three-dimensional model for the enzyme (MerB) in P. fluorescens is proposed, through homology modeling, the characterization at the secondary and tertiary structure level, the characterization of the catalytic domain and the structural motifs present is shown.
Palabras clave : Bioinformatics; homology modelling; organomercurial lyase; Pseudomonas jluorescens.