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
- Corzana, F. 3
- Cuesta, I. 3
- Bastida, A. 3
- Hidalgo, A. 3
- Latorre, Montserrat . 3
- González, C. 2
- García-Junceda, E. 3
- Jiménez-Barbero, J. 1
- Asensio, J.L. 3
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1
Centro de Investigaciones Biológicas
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2
Instituto de Química Física Rocasolano
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3
Instituto de Química Orgánica General
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ISSN: 0947-6539
Argitalpen urtea: 2005
Alea: 11
Zenbakia: 17
Orrialdeak: 5102-5113
Mota: Artikulua
beta Ver similares en nube de resultadosBeste argitalpen batzuk: Chemistry - A European Journal
Laburpena
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.