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1BYJ

GENTAMICIN C1A A-SITE COMPLEX

Summary for 1BYJ
Entry DOI10.2210/pdb1byj/pdb
DescriptorRNA (16S RNA), 2,6-diamino-2,3,4,6-tetradeoxy-alpha-D-erythro-hexopyranose, 3,5-DIAMINO-CYCLOHEXANOL, ... (4 entities in total)
Functional Keywordscomplex (aminoglycoside-ribosomal rna), rna
Total number of polymer chains1
Total formula weight9109.76
Authors
Yoshizawa, S.,Fourmy, D.,Puglisi, J.D. (deposition date: 1998-10-16, release date: 1999-10-29, Last modification date: 2023-12-27)
Primary citationYoshizawa, S.,Fourmy, D.,Puglisi, J.D.
Structural origins of gentamicin antibiotic action.
EMBO J., 17:6437-6448, 1998
Cited by
PubMed Abstract: Aminoglycoside antibiotics that bind to the ribosomal A site cause misreading of the genetic code and inhibit translocation. The clinically important aminoglycoside, gentamicin C, is a mixture of three components. Binding of each gentamicin component to the ribosome and to a model RNA oligonucleotide was studied biochemically and the structure of the RNA complexed to gentamicin C1a was solved using magnetic resonance nuclear spectroscopy. Gentamicin C1a binds in the major groove of the RNA. Rings I and II of gentamicin direct specific RNA-drug interactions. Ring III of gentamicin, which distinguishes this subclass of aminoglycosides, also directs specific RNA interactions with conserved base pairs. The structure leads to a general model for specific ribosome recognition by aminoglycoside antibiotics and a possible mechanism for translational inhibition and miscoding. This study provides a structural rationale for chemical synthesis of novel aminoglycosides.
PubMed: 9822590
DOI: 10.1093/emboj/17.22.6437
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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