The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire.
Cell
; 181(3): 665-673.e10, 2020 04 30.
Article
en En
| MEDLINE
| ID: mdl-32289252
ABSTRACT
A growing number of bacteria are recognized to conduct electrons across their cell envelope, and yet molecular details of the mechanisms supporting this process remain unknown. Here, we report the atomic structure of an outer membrane spanning protein complex, MtrAB, that is representative of a protein family known to transport electrons between the interior and exterior environments of phylogenetically and metabolically diverse microorganisms. The structure is revealed as a naturally insulated biomolecular wire possessing a 10-heme cytochrome, MtrA, insulated from the membrane lipidic environment by embedding within a 26 strand ß-barrel formed by MtrB. MtrAB forms an intimate connection with an extracellular 10-heme cytochrome, MtrC, which presents its hemes across a large surface area for electrical contact with extracellular redox partners, including transition metals and electrodes.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Proteínas de la Membrana Bacteriana Externa
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Proteínas Bacterianas
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Factores de Transcripción
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Proteínas de Unión al ARN
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Transportadoras de Casetes de Unión a ATP
Idioma:
En
Año:
2020
Tipo del documento:
Article