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Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...

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Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...

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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

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Sitios de superficie para la ingeniería de control alostérico en proteínas.

Jeeyeon Lee¹, Madhusudan Natarajan, Vishal C Nashine

¹Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA.

Science (New York, N.Y.)

|October 18, 2008

Resumen

Este resumen es generado por máquina.

Los científicos diseñaron una nueva proteína, PAS-DHFR, al vincular un dominio sensible a la luz con una enzima. Esto crea una proteína controlable que responde a la luz, lo que demuestra un nuevo método para la ingeniería de proteínas.

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Área de la Ciencia:

La bioquímica es la bioquímica.
La ingeniería de proteínas es la ingeniería de proteínas.
Biología Molecular Biología Molecular

Sus antecedentes:

Las familias de proteínas exhiben redes de aminoácidos en coevolución que unen superficies funcionales distantes.
Estas redes sugieren una estrategia para diseñar el control alostérico en proteínas uniéndose a redes intramoleculares.

Objetivo del estudio:

Para probar el concepto de ingeniería de control alostérico mediante la creación de una proteína quimérica.
Para demostrar que la actividad de las proteínas puede ser regulada mediante la conexión de dominios de señalización a las enzimas.

Principales métodos:

Análisis estadístico de familias de proteínas para identificar redes de aminoácidos en coevolución.
Diseño y creación de una proteína quimérica (PAS-DHFR) mediante la fusión de un dominio de señalización vegetal Per/Arnt/Sim (PAS) con la dihidrofolato reductasa (DHFR) de Escherichia coli.

Principales resultados:

La proteína quimérica PAS-DHFR diseñada exhibió actividad catalítica dependiente de la luz sin optimización.
La actividad dependiente de la luz observada dependía del sitio de conexión específico y los mecanismos de señalización conocidos de ambas proteínas progenitoras.

Conclusiones:

PAS-DHFR sirve como una prueba de concepto para la ingeniería de funciones reguladoras en las proteínas.
El diseño de interfaz en sitios alostéricos conservados es una estrategia viable para crear nuevas actividades reguladoras en las proteínas.