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PDBsum entry 4tpc
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Contents |
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218 a.a.
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206 a.a.
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205 a.a.
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150 a.a.
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100 a.a.
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151 a.a.
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129 a.a.
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127 a.a.
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98 a.a.
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117 a.a.
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123 a.a.
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114 a.a.
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96 a.a.
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88 a.a.
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82 a.a.
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80 a.a.
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55 a.a.
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79 a.a.
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85 a.a.
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51 a.a.
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Obsolete entry |
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PDB id:
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| Name: |
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Ribosome
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Title:
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Crystal structure of the e. Coli ribosome bound to flopristin and linopristin. This file contains the 30s subunit of the first 70s ribosome.
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Structure:
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16s rrna. Chain: a. 30s ribosomal protein s2. Chain: b. 30s ribosomal protein s3. Chain: c. 30s ribosomal protein s4. Chain: d. 30s ribosomal protein s5.
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Source:
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Escherichia coli str. K-12 substr. Mds42. Organism_taxid: 1110693. Escherichia coli. Organism_taxid: 83333. Strain: k12. Strain: k12
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Resolution:
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2.80Å
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R-factor:
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0.216
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R-free:
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0.260
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Authors:
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J.Noeske,J.Huang,N.B.Olivier,R.A.Giacobbe,M.Zambrowski,J.H.D.Cate
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Key ref:
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J.Noeske
et al.
(2014).
Synergy of streptogramin antibiotics occurs independently of their effects on translation.
Antimicrob Agents Chemother,
58,
5269-5279.
PubMed id:
DOI:
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Date:
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07-Jun-14
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Release date:
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30-Jul-14
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PROCHECK
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Headers
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References
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P0A7V0
(RS2_ECOLI) -
30S ribosomal protein S2 from Escherichia coli (strain K12)
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Seq: Struc:
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241 a.a.
218 a.a.
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P0A7V3
(RS3_ECOLI) -
30S ribosomal protein S3 from Escherichia coli (strain K12)
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Seq: Struc:
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233 a.a.
206 a.a.
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P0A7V8
(RS4_ECOLI) -
30S ribosomal protein S4 from Escherichia coli (strain K12)
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Seq: Struc:
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206 a.a.
205 a.a.
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P0A7W1
(RS5_ECOLI) -
30S ribosomal protein S5 from Escherichia coli (strain K12)
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Seq: Struc:
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167 a.a.
150 a.a.
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P02358
(RS6_ECOLI) -
30S ribosomal protein S6 from Escherichia coli (strain K12)
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Seq: Struc:
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135 a.a.
100 a.a.
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P02359
(RS7_ECOLI) -
30S ribosomal protein S7 from Escherichia coli (strain K12)
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Seq: Struc:
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179 a.a.
151 a.a.
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P0A7W7
(RS8_ECOLI) -
30S ribosomal protein S8 from Escherichia coli (strain K12)
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Seq: Struc:
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130 a.a.
129 a.a.
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P0A7X3
(RS9_ECOLI) -
30S ribosomal protein S9 from Escherichia coli (strain K12)
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Seq: Struc:
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130 a.a.
127 a.a.
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P0A7R5
(RS10_ECOLI) -
30S ribosomal protein S10 from Escherichia coli (strain K12)
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Seq: Struc:
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103 a.a.
98 a.a.
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P0A7R9
(RS11_ECOLI) -
30S ribosomal protein S11 from Escherichia coli (strain K12)
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Seq: Struc:
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129 a.a.
117 a.a.
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P0A7S3
(RS12_ECOLI) -
30S ribosomal protein S12 from Escherichia coli (strain K12)
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Seq: Struc:
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124 a.a.
123 a.a.
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P0A7S9
(RS13_ECOLI) -
30S ribosomal protein S13 from Escherichia coli (strain K12)
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Seq: Struc:
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118 a.a.
114 a.a.
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P0AG59
(RS14_ECOLI) -
30S ribosomal protein S14 from Escherichia coli (strain K12)
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Seq: Struc:
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101 a.a.
96 a.a.
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P0ADZ4
(RS15_ECOLI) -
30S ribosomal protein S15 from Escherichia coli (strain K12)
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Seq: Struc:
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89 a.a.
88 a.a.
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P0A7T3
(RS16_ECOLI) -
30S ribosomal protein S16 from Escherichia coli (strain K12)
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Seq: Struc:
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82 a.a.
82 a.a.
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P0AG63
(RS17_ECOLI) -
30S ribosomal protein S17 from Escherichia coli (strain K12)
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Seq: Struc:
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84 a.a.
80 a.a.
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P0A7T7
(RS18_ECOLI) -
30S ribosomal protein S18 from Escherichia coli (strain K12)
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Seq: Struc:
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75 a.a.
55 a.a.
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P0A7U3
(RS19_ECOLI) -
30S ribosomal protein S19 from Escherichia coli (strain K12)
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Seq: Struc:
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92 a.a.
79 a.a.
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DOI no:
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Antimicrob Agents Chemother
58:5269-5279
(2014)
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PubMed id:
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| |
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Synergy of streptogramin antibiotics occurs independently of their effects on translation.
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J.Noeske,
J.Huang,
N.B.Olivier,
R.A.Giacobbe,
M.Zambrowski,
J.H.Cate.
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ABSTRACT
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Streptogramin antibiotics are divided into types A and B, which in combination
can act synergistically. We compared the molecular interactions of the
streptogramin combinations Synercid (type A, dalfopristin; type B, quinupristin)
and NXL 103 (type A, flopristin; type B, linopristin) with the Escherichia coli
70S ribosome by X-ray crystallography. We further analyzed the activity of the
streptogramin components individually and in combination. The streptogramin A
and B components in Synercid and NXL 103 exhibit synergistic antimicrobial
activity against certain pathogenic bacteria. However, in transcription-coupled
translation assays, only combinations that include dalfopristin, the
streptogramin A component of Synercid, show synergy. Notably, the
diethylaminoethylsulfonyl group in dalfopristin reduces its activity but is the
basis for synergy in transcription-coupled translation assays before its rapid
hydrolysis from the depsipeptide core. Replacement of the
diethylaminoethylsulfonyl group in dalfopristin by a nonhydrolyzable group may
therefore be beneficial for synergy. The absence of general streptogramin
synergy in transcription-coupled translation assays suggests that the
synergistic antimicrobial activity of streptogramins can occur independently of
the effects of streptogramin on translation.
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');
}
}
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