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Molecular Recognition of Aminoglycoside Antibiotics by Bacterial Defence Proteins: NMR Study of the Structural and Conformational Features of Streptomycin Inactivation by Bacillus subtilis Aminoglycoside‐6‐adenyl Transferase
Author(s) -
Corzana Francisco,
Cuesta Igor,
Bastida Agatha,
Hidalgo Ana,
Latorre Montserrat,
González Carlos,
GarcíaJunceda Eduardo,
JiménezBarbero Jesús,
Asensio Juan Luis.
Publication year - 2005
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200400941
Subject(s) - streptomycin , aminoglycoside , bacillus subtilis , chemistry , antibiotics , moiety , biochemistry , stereochemistry , biology , bacteria , genetics
Abstract 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 approach 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.