<?xml version="1.0" encoding="ISO-8859-1"?><article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance">
<front>
<journal-meta>
<journal-id>0120-2804</journal-id>
<journal-title><![CDATA[Revista Colombiana de Química]]></journal-title>
<abbrev-journal-title><![CDATA[Rev.Colomb.Quim.]]></abbrev-journal-title>
<issn>0120-2804</issn>
<publisher>
<publisher-name><![CDATA[Departamento de Química,  Universidad Nacional de Colombia.]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S0120-28042022000100014</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[Modelamiento in silica de la liasa organomercurial (MerB) de Pseudamanas fluarescens]]></article-title>
<article-title xml:lang="en"><![CDATA[In silico modeling of Pseudomonas fluoresceins organomercurial lyase (MerB)]]></article-title>
<article-title xml:lang="pt"><![CDATA[Modelagem in silica da liase organomercurial (MerB) de Pseudamanas fluarescens]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[D-Kerynd]]></surname>
<given-names><![CDATA[Barona]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Duverney]]></surname>
<given-names><![CDATA[Gaviria]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Libre Facultad de Ciencias de la salud exacta y Naturales ]]></institution>
<addr-line><![CDATA[Pereira ]]></addr-line>
<country>Colombia</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>04</month>
<year>2022</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>04</month>
<year>2022</year>
</pub-date>
<volume>51</volume>
<numero>1</numero>
<fpage>14</fpage>
<lpage>23</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_arttext&amp;pid=S0120-28042022000100014&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_abstract&amp;pid=S0120-28042022000100014&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_pdf&amp;pid=S0120-28042022000100014&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen El modelamiento ¡n silíco ha sido de gran contribución en los procesos proteómicos, desarrollando estructuras de las secuencias proteicas ya existentes, que por motivos de altos costos y las diferentes tecnologías necesarias para el desarrollo de estas metodologías, se encuentran deficientes en el número de modelamientos de proteínas disponibles. Entre aquellas secuencias con carencia de estructura proteica se encuentra la proteína liasa organomercurial (MerB) de Pseudomonas /luorescens, importante en la resistencia al mercurio. En el presente artículo se analizó tanto estructural como funcionalmente la proteína MerB en Pseudomonas jluorescens, utilizando la herramienta de la química estructural "modelamiento por homología" mediante plataformas bioinformáticas, con el fin de obtener un modelo que represente la estructura 3D más precisa y que capturen las mejores variantes estructurales entre todas las posibles conformaciones de las proteínas en la familia. En este trabajo, se desarrolló un método comparativo de la secuencia estudiada con las reportadas en las bases de datos para las proteínas MerB del género Pseudomonas. Se propone un modelo tridimensional para la enzima (MerB) en P. jluorescens, mediante el modelamiento por homología, se muestra la caracterización en la estructura secundaria, terciaria, la caracterización del dominio catalítico y los motivos estructurales presentes.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract 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.]]></p></abstract>
<abstract abstract-type="short" xml:lang="pt"><p><![CDATA[Resumo A modelagem in silico tem dado um grande contributo para os processos proteómicos, desenvolvendo estruturas de sequências de proteínas já existentes, as quais, pelos elevados custos e pelas diferentes tecnologias necessárias ao desenvolvimento destas metodologias, são deficientes no número de modelos de proteínas disponíveis. Entre as sequências sem estrutura protéica está a proteína organomercurial liase (MerB) de Pseudomonas fluorescens, importante na resistência ao mercúrio. Neste artigo, a proteína MerB em Pseudomonas fluorescens foi analisada estrutural e funcionalmente, usando a ferramenta de química estrutural "modelagem de homologia" usando plataformas de bioinformática, a fim de obter um modelo que represente a estrutura 3D mais precisa e que capture as melhores variantes estruturais. entre todas as conformações possíveis das proteínas da família. Neste trabalho, foi desenvolvido um método comparativo da sequência estudada com aqueles relatados em bancos de dados para proteínas MerB do gênero Pseudomonas. Um modelo tridimensional para a enzima (MerB) em P. fluorescens é proposto, através de modelagem por homologia, a caracterização em nível de estrutura secundária e terciária, a caracterização do domínio catalítico e os motivos estruturais presentes são mostradas.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[bioinformática]]></kwd>
<kwd lng="es"><![CDATA[modelado por homología]]></kwd>
<kwd lng="es"><![CDATA[organomercurial liasa]]></kwd>
<kwd lng="es"><![CDATA[Pseudomonas fluorescens]]></kwd>
<kwd lng="en"><![CDATA[Bioinformatics]]></kwd>
<kwd lng="en"><![CDATA[homology modelling]]></kwd>
<kwd lng="en"><![CDATA[organomercurial lyase]]></kwd>
<kwd lng="en"><![CDATA[Pseudomonas jluorescens]]></kwd>
<kwd lng="pt"><![CDATA[bioinformática]]></kwd>
<kwd lng="pt"><![CDATA[modelagem de homologia]]></kwd>
<kwd lng="pt"><![CDATA[organomercurial Liasa]]></kwd>
<kwd lng="pt"><![CDATA[Pseudomonas fluorescens]]></kwd>
</kwd-group>
</article-meta>
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