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Ribosome PDB-id
1fjg
Biological unit* = asymmetric unit, as shown
(*as deduced by PQS)
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Contents
Description
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PROCHECK
Protein chains
237 a.a. *
206 a.a. *
208 a.a. *
150 a.a. *
101 a.a. *
155 a.a. *
138 a.a. *
127 a.a. *
98 a.a. *
119 a.a. *
125 a.a. *
125 a.a. *
60 a.a. *
88 a.a. *
83 a.a. *
104 a.a. *
73 a.a. *
84 a.a. *
99 a.a. *
24 a.a. *
DNA/RNA
Ligands
PAR
SCM
SRY
Metal ions
_MG ×96
_ZN ×2

* Residue conservation analysis
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PDB id: 1fjg
Name: Ribosome
Title: Structure of the thermus thermophilus 30s ribosomal subunit in complex with the antibiotics streptomycin, spectinomycin, and paromomycin

Structure:
16s ribosomal RNA. Chain: a. Fragment of messenger RNA. Chain: x. 30s ribosomal protein s2. Chain: b. 30s ribosomal protein s3. Chain: c. 30s ribosomal protein s4.

Source:
Thermus thermophilus. Organism_taxid: 274. Organism_taxid: 274

Biological unit:
22mer (from PQS)

UniProt:
Chain B: P80371 (RS2_THET8)
Pfam   ArchSchema ?
Seq: 256 a.a.
Struc: 237 a.a.

Chain C: P80372 (RS3_THET8)
Pfam   ArchSchema ?
Seq: 239 a.a.
Struc: 206 a.a.

Chain D: P80373 (RS4_THET8)
Pfam   ArchSchema ?
Seq: 209 a.a.
Struc: 208 a.a.*

Chain E: Q5SHQ5 (RS5_THET8)
Pfam   ArchSchema ?
Seq: 162 a.a.
Struc: 150 a.a.

Chain F: Q5SLP8 (RS6_THET8)
Pfam   ArchSchema ?
Seq: 101 a.a.
Struc: 101 a.a.

Chain G: P17291 (RS7_THET8)
Pfam   ArchSchema ?
Seq: 156 a.a.
Struc: 155 a.a.

Chain H: Q5SHQ2 (RS8_THET8)
Pfam   ArchSchema ?
Seq: 138 a.a.
Struc: 138 a.a.

Chain I: P80374 (RS9_THET8)
Pfam   ArchSchema ?
Seq: 128 a.a.
Struc: 127 a.a.*

Chain J: Q5SHN7 (RS10_THET8)
Pfam   ArchSchema ?
Seq: 105 a.a.
Struc: 98 a.a.

Chain K: P80376 (RS11_THET8)
Pfam   ArchSchema ?
Seq: 129 a.a.
Struc: 119 a.a.

Chain L: Q5SHN3 (RS12_THET8)
Pfam   ArchSchema ?
Seq: 132 a.a.
Struc: 125 a.a.

Chain M: P80377 (RS13_THET8)
Pfam   ArchSchema ?
Seq: 126 a.a.
Struc: 125 a.a.

Chain N: Q5SHQ1 (RS14Z_THET8)
Pfam   ArchSchema ?
Seq: 61 a.a.
Struc: 60 a.a.

Chain O: Q5SJ76 (RS15_THET8)
Pfam   ArchSchema ?
Seq: 89 a.a.
Struc: 88 a.a.

Chain P: Q5SJH3 (RS16_THET8)
Pfam   ArchSchema ?
Seq: 88 a.a.
Struc: 83 a.a.

Chain Q: Q5SHP7 (RS17_THET8)
Pfam   ArchSchema ?
Seq: 105 a.a.
Struc: 104 a.a.*

Chain R: Q5SLQ0 (RS18_THET8)
Pfam   ArchSchema ?
Seq: 88 a.a.
Struc: 73 a.a.*

Chain S: Q5SHP2 (RS19_THET8)
Pfam   ArchSchema ?
Seq: 93 a.a.
Struc: 84 a.a.

Chain T: P80380 (RS20_THET8)
Pfam   ArchSchema ?
Seq: 106 a.a.
Struc: 99 a.a.*

Chain V: Q5SIH3 (RSHX_THET8)
Pfam  
Seq: 27 a.a.
Struc: 24 a.a.
Key:    PfamA domain  PfamB domain
 Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

Resolution:
3.00Å

R-factor:
0.221

R-free:
0.255

Authors:
A.P.Carter,W.M.Clemons Jr.,D.E.Brodersen,B.T.Wimberly, R.J.Morgan-Warren,V.Ramakrishnan

Key ref:
A.P.Carter et al. (2000). Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics.. Nature, 407, 340-348. [PubMed id: 11014183] [DOI: 10.1038/35030019]

Date:
08-Aug-00

Release date:
25-Sep-00

Related entries:
1qd7
earlier partial model of the 30s particle
1fjf
native structure of the 30s particle
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    Key reference    
 
 
DOI no: 10.1038/35030019 Nature 407:340-348 (2000)
PubMed id: 11014183  
 
 
Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics.
A.P.Carter, W.M.Clemons, D.E.Brodersen, R.J.Morgan-Warren, B.T.Wimberly, V.Ramakrishnan.
 
  ABSTRACT  
 
The 30S ribosomal subunit has two primary functions in protein synthesis. It discriminates against aminoacyl transfer RNAs that do not match the codon of messenger RNA, thereby ensuring accuracy in translation of the genetic message in a process called decoding. Also, it works with the 50S subunit to move the tRNAs and associated mRNA by precisely one codon, in a process called translocation. Here we describe the functional implications of the high-resolution 30S crystal structure presented in the accompanying paper, and infer details of the interactions between the 30S subunit and its tRNA and mRNA ligands. We also describe the crystal structure of the 30S subunit complexed with the antibiotics paromomycin, streptomycin and spectinomycin, which interfere with decoding and translocation. This work reveals the structural basis for the action of these antibiotics, and leads to a model for the role of the universally conserved 16S RNA residues A1492 and A1493 in the decoding process.
 
  Selected figure(s)  
 
Figure 4.
Figure 4: Interaction of spectinomycin with the 30S ribosomal subunit. a, Difference Fourier maps showing the binding site of spectinomycin in helix 34. b, Chemical structure of spectinomycin, showing interactions of the various groups with specific residues of 30S. c, The spectinomycin-binding site, showing its location at a pivotal point in the head of the 30S subunit. d, Inset showing spectinomycin in a space-filling model, and the location of its binding site on the 30S.
Figure 5.
Figure 5: Interaction of streptomycin with the 30S ribosomal subunit. a, Difference Fourier maps showing the binding site of streptomycin. Mutations in ribosomal protein S12 that confer resistance are shown in red. b, Chemical structure of streptomycin, showing interactions of the various groups with specific residues of the ribosome. c, The streptomycin-binding site, showing its interaction with H27, the 530 loop (H18), H44 and ribosomal protein S12. d, A view of the 30S showing streptomycin in a space-filling model, and the surrounding RNA and protein elements.
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (2000, 407, 340-348) copyright 2000.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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  Mol Microbiol, 71, 1239-1249.  
19104019 G.Wang, T.Inaoka, S.Okamoto, and K.Ochi (2009).
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PDB codes: 3ham 3hav
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Translation at the single-molecule level.
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Pentamidine binds to tRNA through non-specific hydrophobic interactions and inhibits aminoacylation and translation.
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NMR structure of the peptidyl transferase RNA inhibitor antibiotic amicetin.
  Magn Reson Chem, 45, 133-141.  
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Kinetically competent intermediates in the translocation step of protein synthesis.
  Mol Cell, 25, 519-529.  
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The frequency of translational misreading errors in E. coli is largely determined by tRNA competition.
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Differentiating between near- and non-cognate codons in Saccharomyces cerevisiae.
  PLoS ONE, 2, e517.  
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Back to the future: the ribosome as an antibiotic target.
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Source-sink dynamics shape the evolution of antibiotic resistance and its pleiotropic fitness cost.
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Inhibition of antiassociation activity of translation initiation factor 3 by paromomycin.
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In vitro prediction of stop-codon suppression by intravenous gentamicin in patients with cystic fibrosis: a pilot study.
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Base-flipping dynamics in a DNA hairpin processing reaction.
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17705310 J.Kondo, M.Hainrichson, I.Nudelman, D.Shallom-Shezifi, C.M.Barbieri, D.S.Pilch, E.Westhof, and T.Baasov (2007).
Differential selectivity of natural and synthetic aminoglycosides towards the eukaryotic and prokaryotic decoding A sites.
  Chembiochem, 8, 1700-1709.
PDB codes: 2o3v 2o3w 2o3x 2o3y
17505105 J.Kondo, T.Sunami, and A.Takénaka (2007).
The structure of a d(gcGAACgc) duplex containing two consecutive bulged A residues in both strands suggests a molecular switch.
  Acta Crystallogr D Biol Crystallogr, 63, 673-681.
PDB code: 2got
17384190 J.R.Nodwell (2007).
Novel links between antibiotic resistance and antibiotic production.
  J Bacteriol, 189, 3683-3685.  
17875999 J.Wachino, K.Shibayama, H.Kurokawa, K.Kimura, K.Yamane, S.Suzuki, N.Shibata, Y.Ike, and Y.Arakawa (2007).
Novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides.
  Antimicrob Agents Chemother, 51, 4401-4409.  
16892199 J.Zhou, G.Wang, L.H.Zhang, and X.S.Ye (2007).
Modifications of aminoglycoside antibiotics targeting RNA.
  Med Res Rev, 27, 279-316.  
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Isolation and characterization of sporulation-initiation mutation in the Bacillus subtilis prfB gene.
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Identification of the RsmG methyltransferase target as 16S rRNA nucleotide G527 and characterization of Bacillus subtilis rsmG mutants.
  J Bacteriol, 189, 6068-6073.  
17384192 K.Nishimura, T.Hosaka, S.Tokuyama, S.Okamoto, and K.Ochi (2007).
Mutations in rsmG, encoding a 16S rRNA methyltransferase, result in low-level streptomycin resistance and antibiotic overproduction in Streptomyces coelicolor A3(2).
  J Bacteriol, 189, 3876-3883.  
17587668 K.Ochi (2007).
From microbial differentiation to ribosome engineering.
  Biosci Biotechnol Biochem, 71, 1373-1386.  
17704156 K.Réblová, E.Fadrná, J.Sarzynska, T.Kulinski, P.Kulhánek, E.Ennifar, J.Koca, and J.Sponer (2007).
Conformations of flanking bases in HIV-1 RNA DIS kissing complexes studied by molecular dynamics.
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17407165 K.S.Sandhu, and D.Dash (2007).
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17592474 K.Wang, H.Neumann, S.Y.Peak-Chew, and J.W.Chin (2007).
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17159993 L.Cochella, J.L.Brunelle, and R.Green (2007).
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PDB codes: 2qal 2qam 2qan 2qao 2qb9 2qba 2qbb 2qbc 2qbd 2qbe 2qbf 2qbg 2qbh 2qbi 2qbj 2qbk 2z4k 2z4l 2z4m 2z4n
17394189 M.D.Disney, and J.L.Childs-Disney (2007).
Using selection to identify and chemical microarray to study the RNA internal loops recognized by 6'-N-acylated kanamycin A.
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17210778 M.Goswami, S.H.Mangoli, and N.Jawali (2007).
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17804668 M.Kaczanowska, and M.Rydén-Aulin (2007).
Ribosome biogenesis and the translation process in Escherichia coli.
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17564727 M.O'connor (2007).
Interaction between the ribosomal subunits: 16S rRNA suppressors of the lethal DeltaA1916 mutation in the 23S rRNA of Escherichia coli.
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17323326 P.C.Anderson, and S.Mecozzi (2007).
Minimum sequence requirements for the binding of paromomycin to the rRNA decoding site A.
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17391549 P.C.Bevilacqua, A.L.Cerrone-Szakal, and N.A.Siegfried (2007).
Insight into the functional versatility of RNA through model-making with applications to data fitting.
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Monitoring aminoglycoside-induced conformational changes in 16S rRNA through acrylamide quenching.
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The structures of antibiotics bound to the E site region of the 50 S ribosomal subunit of Haloarcula marismortui: 13-deoxytedanolide and girodazole.
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PDB codes: 2otj 2otl
17766247 S.N.Hobbie, S.K.Kalapala, S.Akshay, C.Bruell, S.Schmidt, S.Dabow, A.Vasella, P.Sander, and E.C.Böttger (2007).
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17539821 S.O.Meroueh, and S.Mobashery (2007).
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16990269 A.Kubarenko, P.Sergiev, W.Wintermeyer, O.Dontsova, and M.V.Rodnina (2006).
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16721598 A.W.Strittmatter, C.Fischer, M.Kleinschmidt, and G.H.Braus (2006).
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16495252 B.L.Makepeace, L.Rodgers, and A.J.Trees (2006).
Rate of elimination of Wolbachia pipientis by doxycycline in vitro increases following drug withdrawal.
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16998486 B.S.Schuwirth, J.M.Day, C.W.Hau, G.R.Janssen, A.E.Dahlberg, J.H.Cate, and A.Vila-Sanjurjo (2006).
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PDB codes: 1vs5 1vs6 1vs7 1vs8
17129165 C.Hyeon, R.I.Dima, and D.Thirumalai (2006).
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16390446 D.Büttner, C.Lorenz, E.Weber, and U.Bonas (2006).
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16436695 D.Criswell, V.L.Tobiason, J.S.Lodmell, and D.S.Samuels (2006).
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16957210 D.Dailidiene, G.Dailide, D.Kersulyte, and D.E.Berg (2006).
Contraselectable streptomycin susceptibility determinant for genetic manipulation and analysis of Helicobacter pylori.
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16679451 E.Ennifar, J.C.Paillart, A.Bodlenner, P.Walter, J.M.Weibel, A.M.Aubertin, P.Pale, P.Dumas, and R.Marquet (2006).
Targeting the dimerization initiation site of HIV-1 RNA with aminoglycosides: from crystal to cell.
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PDB codes: 2fcx 2fcy 2fcz 2fd0
17381338 E.M.Youngman, L.Cochella, J.L.Brunelle, S.He, and R.Green (2006).
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The antibiotic kasugamycin mimics mRNA nucleotides to destabilize tRNA binding and inhibit canonical translation initiation.
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PDB code: 2hhh
16881035 F.von Nussbaum, M.Brands, B.Hinzen, S.Weigand, and D.Häbich (2006).
Antibacterial natural products in medicinal chemistry--exodus or revival?
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16717405 H.Yoneyama, and R.Katsumata (2006).
Antibiotic resistance in bacteria and its future for novel antibiotic development.
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16724458 J.Donarski, C.Shammas, R.Banks, and V.Ramesh (2006).
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PDB code: 2fqn
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Crystal structure of the Homo sapiens cytoplasmic ribosomal decoding site complexed with apramycin.
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PDB code: 2g5k
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Aminoglycoside-quinacridine conjugates: towards recognition of the P6.1 element of telomerase RNA.
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Structure of the 70S ribosome complexed with mRNA and tRNA.
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PDB codes: 2j00 2j01 2j02 2j03
17012271 N.E.McCrate, M.E.Varner, K.I.Kim, and M.C.Nagan (2006).
Molecular dynamics simulations of human tRNA Lys,3 UUU: the role of modified bases in mRNA recognition.
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Drugs, their targets and the nature and number of drug targets.
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17000775 R.Rakauskaite, and J.D.Dinman (2006).
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16679452 S.Lemieux, and F.Major (2006).
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Antibiotics and the ribosome.
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Structural basis for mRNA and tRNA positioning on the ribosome.
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PDB codes: 2i2p 2i2t 2i2u 2i2v
16557321 Y.Rao, A.Venot, E.E.Swayze, R.H.Griffey, and G.J.Boons (2006).
Trisaccharide mimetics of the aminoglycoside antibiotic neomycin.
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Antibiotics targeting ribosomes: resistance, selectivity, synergism and cellular regulation.
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PDB codes: 2esi 2esj 2et3 2et4 2et5 2et8
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The social life of ribosomal proteins.
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A functional relationship between helix 1 and the 900 tetraloop of 16S ribosomal RNA within the bacterial ribosome.
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Molecular recognition of RNA by neomycin and a restricted neomycin derivative.
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PDB codes: 1zx7 1zz5 2a04
16199759 H.Liang, L.F.Landweber, and J.R.Fresco (2005).
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16095538 I.Majumdar, S.S.Krishna, and N.V.Grishin (2005).
PALSSE: a program to delineate linear secondary structural elements from protein structures.
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Severity of the streptomycin resistance and streptomycin dependence phenotypes of ribosomal protein S12 of Thermus thermophilus depends on the identity of highly conserved amino acid residues.
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15980485 J.Kleinjung, and F.Fraternali (2005).
POPSCOMP: an automated interaction analysis of biomolecular complexes.
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15952884 J.M.Ogle, and V.Ramakrishnan (2005).
Structural insights into translational fidelity.
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16261170 J.Poehlsgaard, and S.Douthwaite (2005).
The bacterial ribosome as a target for antibiotics.
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15756640 J.Sandbrink, D.Ossipov, H.Aström, and R.Strömberg (2005).
Investigation of potential RNA bulge stabilizing elements.
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Global transcriptional response of Bacillus subtilis to treatment with subinhibitory concentrations of antibiotics that inhibit protein synthesis.
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