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PDBsum entry 1yi2
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Contents |
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237 a.a.
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337 a.a.
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246 a.a.
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140 a.a.
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172 a.a.
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119 a.a.
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29 a.a.
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160 a.a.
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70 a.a.
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142 a.a.
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132 a.a.
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145 a.a.
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194 a.a.
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186 a.a.
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115 a.a.
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143 a.a.
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95 a.a.
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150 a.a.
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81 a.a.
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119 a.a.
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53 a.a.
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65 a.a.
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154 a.a.
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82 a.a.
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142 a.a.
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73 a.a.
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56 a.a.
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46 a.a.
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92 a.a.
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 _CL
×22
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 _NA
×86
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_MG
×116
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 _CD
×5
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 __K
×2
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References listed in PDB file
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Key reference
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Title
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Structures of mlsbk antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance.
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Authors
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D.Tu,
G.Blaha,
P.B.Moore,
T.A.Steitz.
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Ref.
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Cell, 2005,
121,
257-270.
[DOI no: ]
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PubMed id
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Abstract
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Crystal structures of H. marismortui large ribosomal subunits containing the
mutation G2099A (A2058 in E. coli) with erythromycin, azithromycin, clindamycin,
virginiamycin S, and telithromycin bound explain why eubacterial ribosomes
containing the mutation A2058G are resistant to them. Azithromycin binds almost
identically to both G2099A and wild-type subunits, but the erythromycin affinity
increases by more than 10(4)-fold, implying that desolvation of the N2 of G2099
accounts for the low wild-type affinity for macrolides. All macrolides bind
similarly to the H. marismortui subunit, but their binding differs significantly
from what has been reported in the D. radioidurans subunit. The synergy in the
binding of streptogramins A and B appears to result from a reorientation of the
base of A2103 (A2062, E. coli) that stacks between them. The structure of large
subunit containing a three residue deletion mutant of L22 shows a change in the
L22 structure and exit tunnel shape that illuminates its macrolide resistance
phenotype.
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Figure 5.
Figure 5. A Model of the Eight N-Terminal Amino Acids of
the ermC Operon Leader Peptide Bound at the PTC End of the
Peptide Exit Tunnel
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Figure 6.
Figure 6. Differences between Models of MLS[B]K Antibiotics
Bound to the H. marismortui (Hma) and D. radiodurans (Dra)
Ribosomes
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2005,
121,
257-270)
copyright 2005.
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