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La estructura en forma de rosquilla de una muramidasa bacteriana revelada por la cristalografía de rayos X
A M Thunnissen1, A J Dijkstra, K H Kalk
1BIOSON Research Institute, Department of Chemistry, University of Groningen, The Netherlands.
Nature
|February 24, 1994
Resumen
Los investigadores determinaron la estructura de una enzima bacteriana, la transglicosilasa lítica soluble (SLT), que degrada el peptidoglicano. Este hallazgo ofrece nuevos objetivos para el desarrollo de antibióticos distintos de la penicilina.
Área de la Ciencia:
- Microbiología Microbiología.
- Biología Estructural Biología estructural.
- La bioquímica es la bioquímica.
Sus antecedentes:
- La integridad de la pared celular bacteriana depende de la síntesis de peptidoglicano y las enzimas de degradación.
- La penicilina se dirige a las enzimas involucradas en el enlace cruzado del peptidoglicano.
- Las enzimas que actúan sobre los enlaces glucósidos no son inhibidas por la penicilina, presentando objetivos antibióticos alternativos.
Objetivo del estudio:
- Para determinar la estructura de rayos X de Escherichia coli disoluble lítico transglicosilasa (SLT). para determinar la estructura de rayos X de Escherichia coli disoluble lítico transglicosilasa (SLT). para determinar la estructura de rayos X de Escherichia coli disoluble litico transglicosilasa (SLT). para determinar la estructura de rayos X de Escherichia coli disoluble (SLT). para determinar la estructura de rayos X de Escherichia coli. para determinar la estructura de rayos X de Escherichia coli.
- Identificar objetivos potenciales para nuevos antibióticos distintos de los beta-lactamas.
Principales métodos:
- Se utilizó la cristalografía de rayos X para determinar la estructura tridimensional de SLT.
- La mutagenesis dirigida al sitio se empleó para investigar la función de la enzima.
- Se llevaron a cabo estudios de unión a inhibidores cristalográficos.
Principales resultados:
- La estructura de SLT reveló un anillo único "superhelical" de hélices alfa.
- Se identificó un dominio separado que se parece al pliegue de la lisozima.
- Se confirmó que el dominio similar a la lisozima contenía el sitio activo de SLT.
Conclusiones:
- La aclaración estructural de SLT proporciona información sobre los mecanismos de degradación del peptidoglicano.
- El sitio activo identificado en el dominio de tipo lisozima es un objetivo potencial para el desarrollo de nuevos fármacos antibacterianos.
- Dirigirse a SLT ofrece una estrategia para crear antibióticos efectivos contra las bacterias resistentes a la penicilina.
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