Molecular recognition of aminoglycoside antibiotics by bacterial defense proteins: NMR study of the structural and conformational features of streptomycin inactivation by bacillus subtilis Aminoglycoside-6-adenyl Transferase

  1. Corzana, F. 3
  2. Cuesta, I. 3
  3. Bastida, A. 3
  4. Hidalgo, A. 3
  5. Latorre, Montserrat . 3
  6. González, C. 2
  7. García-Junceda, E. 3
  8. Jiménez-Barbero, J. 1
  9. Asensio, J.L. 3
  1. 1 Centro de Investigaciones Biológicas
    info

    Centro de Investigaciones Biológicas

    Madrid, España

    ROR https://ror.org/04advdf21

  2. 2 Instituto de Química Física Rocasolano
    info

    Instituto de Química Física Rocasolano

    Madrid, España

    ROR https://ror.org/03xk60j79

  3. 3 Instituto de Química Orgánica General
    info

    Instituto de Química Orgánica General

    Madrid, España

    ROR https://ror.org/05e0q7s59

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Revista:
Chemistry - A European Journal

ISSN: 0947-6539

Ano de publicación: 2005

Volume: 11

Número: 17

Páxinas: 5102-5113

Tipo: Artigo

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DOI: 10.1002/CHEM.200400941 PMID: 15984036 SCOPUS: 2-s2.0-24344463899 GOOGLE SCHOLAR

Outras publicacións en: Chemistry - A European Journal

Repositorio institucional: lock_openAcceso aberto Editor

Resumo

The molecular recognition of streptomycin by Bacillus subtilis aminoglycoside-6-adenyl transferase has been analysed by a combination of NMR techniques and molecular dynamic simulations. This protein inactivates streptomycin by transferring an adenyl group to position six of the streptidine moiety. Our combined ap-proach provides valuable information about the bioactive conformation for both the antibiotic and ATP and shows that the molecular recognition process for streptomycin involves a conformational selection phenomenon. The binding epitope for both ligands has also been analysed by 1D-STD experiments. Finally, the specificity of the recognition process with respect to the aminoglycoside and to the nucleotide has been studied. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.