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The structure of a hibernating ribosome in a Lyme disease pathogen.
Sharma, Manjuli R; Manjari, Swati R; Agrawal, Ekansh K; Keshavan, Pooja; Koripella, Ravi K; Majumdar, Soneya; Marcinkiewicz, Ashley L; Lin, Yi-Pin; Agrawal, Rajendra K; Banavali, Nilesh K.
Afiliación
  • Sharma MR; Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY, USA.
  • Manjari SR; Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY, USA.
  • Agrawal EK; Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY, USA.
  • Keshavan P; University of California at Berkeley, Berkeley, CA, USA.
  • Koripella RK; Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY, USA.
  • Majumdar S; Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY, USA.
  • Marcinkiewicz AL; Apkarian Integrated Electron Microscopy Core, Emory University, Atlanta, GA, USA.
  • Lin YP; Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY, USA.
  • Agrawal RK; Division of Infectious Diseases, Wadsworth Center, New York State Department of Health, Albany, NY, USA.
  • Banavali NK; Division of Infectious Diseases, Wadsworth Center, New York State Department of Health, Albany, NY, USA.
Nat Commun ; 14(1): 6961, 2023 10 31.
Article en En | MEDLINE | ID: mdl-37907464
The spirochete bacterial pathogen Borrelia (Borreliella) burgdorferi (Bbu) affects more than 10% of the world population and causes Lyme disease in about half a million people in the US annually. Therapy for Lyme disease includes antibiotics that target the Bbu ribosome. Here we present the structure of the Bbu 70S ribosome obtained by single particle cryo-electron microscopy at 2.9 Å resolution, revealing a bound hibernation promotion factor protein and two genetically non-annotated ribosomal proteins bS22 and bL38. The ribosomal protein uL30 in Bbu has an N-terminal α-helical extension, partly resembling the mycobacterial bL37 protein, suggesting evolution of bL37 and a shorter uL30 from a longer uL30 protein. Its analogy to proteins uL30m and mL63 in mammalian mitochondrial ribosomes also suggests a plausible evolutionary pathway for expansion of protein content in mammalian mitochondrial ribosomes. Computational binding free energy predictions for antibiotics reflect subtle distinctions in antibiotic-binding sites in the Bbu ribosome. Discovery of these features in the Bbu ribosome may enable better ribosome-targeted antibiotic design for Lyme disease treatment.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Enfermedad de Lyme Límite: Animals / Humans Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Enfermedad de Lyme Límite: Animals / Humans Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido