4P20
Crystal structures of the bacterial ribosomal decoding site complexed with amikacin
Replaces: 2G5QSummary for 4P20
Entry DOI | 10.2210/pdb4p20/pdb |
Descriptor | 5'-R(*UP*UP*GP*CP*GP*UP*CP*AP*CP*AP*CP*CP*GP*GP*UP*GP*AP*AP*GP*UP*CP*GP*C)-3', (2S)-N-[(1R,2S,3S,4R,5S)-4-[(2R,3R,4S,5S,6R)-6-(aminomethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-5-azanyl-2-[(2S,3R,4S,5S ,6R)-4-azanyl-6-(hydroxymethyl)-3,5-bis(oxidanyl)oxan-2-yl]oxy-3-oxidanyl-cyclohexyl]-4-azanyl-2-oxidanyl-butanamide (3 entities in total) |
Functional Keywords | aminoglycoside, haba group, ribosomal decoding site, x-ray analysis, rna, amikacin, rna-antibiotic complex, rna/antibiotic |
Biological source | synthetic construct |
Total number of polymer chains | 2 |
Total formula weight | 15882.02 |
Authors | Kondo, J.,Francois, B.,Russell, R.J.M.,Murray, J.B.,Westhof, E. (deposition date: 2014-02-28, release date: 2014-05-07, Last modification date: 2023-12-27) |
Primary citation | Kondo, J.,Francois, B.,Russell, R.J.,Murray, J.B.,Westhof, E. Crystal structure of the bacterial ribosomal decoding site complexed with amikacin containing the gamma-amino-alpha-hydroxybutyryl (haba) group. Biochimie, 88:1027-1031, 2006 Cited by PubMed Abstract: Amikacin is the 4,6-linked aminoglycoside modified at position N1 of the 2-deoxystreptamine ring (ring II) by the L-haba group. In the present study, the crystal structure of a complex between oligonucleotide containing the bacterial ribosomal A site and amikacin has been solved at 2.7 A resolution. Amikacin specifically binds to the A site in practically the same way as its parent compound kanamycin. In addition, the L-haba group interacts with the upper side of the A site through two direct contacts, O2*...H-N4(C1496) and N4*-H...O6(G1497). The present crystal structure shows how the introduction of the L-haba group on ring II of aminoglycoside is an effective mutation for obtaining a higher affinity to the bacterial A site. PubMed: 16806634DOI: 10.1016/j.biochi.2006.05.017 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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