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protein dna_rna ligands metals Protein-protein interface(s) links
Ribosome PDB id
1fjg
Jmol
Contents
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
Metals
_MG ×96
_ZN ×2
* Residue conservation analysis
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
Biol. unit: 22mer (from PQS)
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    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P80371  (RS2_THET8) -  30S ribosomal protein S2
Seq:
Struc:
256 a.a.
237 a.a.
Protein chain
Pfam   ArchSchema ?
P80372  (RS3_THET8) -  30S ribosomal protein S3
Seq:
Struc:
239 a.a.
206 a.a.
Protein chain
Pfam   ArchSchema ?
P80373  (RS4_THET8) -  30S ribosomal protein S4
Seq:
Struc:
209 a.a.
208 a.a.*
Protein chain
Pfam   ArchSchema ?
Q5SHQ5  (RS5_THET8) -  30S ribosomal protein S5
Seq:
Struc:
162 a.a.
150 a.a.
Protein chain
Pfam   ArchSchema ?
Q5SLP8  (RS6_THET8) -  30S ribosomal protein S6
Seq:
Struc:
101 a.a.
101 a.a.
Protein chain
Pfam   ArchSchema ?
P17291  (RS7_THET8) -  30S ribosomal protein S7
Seq:
Struc:
156 a.a.
155 a.a.
Protein chain
Pfam   ArchSchema ?
Q5SHQ2  (RS8_THET8) -  30S ribosomal protein S8
Seq:
Struc:
138 a.a.
138 a.a.
Protein chain
Pfam   ArchSchema ?
P80374  (RS9_THET8) -  30S ribosomal protein S9
Seq:
Struc:
128 a.a.
127 a.a.*
Protein chain
Pfam   ArchSchema ?
Q5SHN7  (RS10_THET8) -  30S ribosomal protein S10
Seq:
Struc:
105 a.a.
98 a.a.
Protein chain
Pfam   ArchSchema ?
P80376  (RS11_THET8) -  30S ribosomal protein S11
Seq:
Struc:
129 a.a.
119 a.a.
Protein chain
Pfam   ArchSchema ?
Q5SHN3  (RS12_THET8) -  30S ribosomal protein S12
Seq:
Struc:
132 a.a.
125 a.a.
Protein chain
Pfam   ArchSchema ?
P80377  (RS13_THET8) -  30S ribosomal protein S13
Seq:
Struc:
126 a.a.
125 a.a.
Protein chain
Pfam   ArchSchema ?
Q5SHQ1  (RS14Z_THET8) -  30S ribosomal protein S14 type Z
Seq:
Struc:
61 a.a.
60 a.a.
Protein chain
Pfam   ArchSchema ?
Q5SJ76  (RS15_THET8) -  30S ribosomal protein S15
Seq:
Struc:
89 a.a.
88 a.a.
Protein chain
Pfam   ArchSchema ?
Q5SJH3  (RS16_THET8) -  30S ribosomal protein S16
Seq:
Struc:
88 a.a.
83 a.a.
Protein chain
Pfam   ArchSchema ?
Q5SHP7  (RS17_THET8) -  30S ribosomal protein S17
Seq:
Struc:
105 a.a.
104 a.a.*
Protein chain
Pfam   ArchSchema ?
Q5SLQ0  (RS18_THET8) -  30S ribosomal protein S18
Seq:
Struc:
88 a.a.
73 a.a.*
Protein chain
Pfam   ArchSchema ?
Q5SHP2  (RS19_THET8) -  30S ribosomal protein S19
Seq:
Struc:
93 a.a.
84 a.a.
Protein chain
Pfam   ArchSchema ?
P80380  (RS20_THET8) -  30S ribosomal protein S20
Seq:
Struc:
106 a.a.
99 a.a.*
Protein chain
Pfam   ArchSchema ?
Q5SIH3  (RSHX_THET8) -  30S ribosomal protein Thx
Seq:
Struc:
27 a.a.
24 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     intracellular   4 terms 
  Biological process     translation   1 term 
  Biochemical function     structural constituent of ribosome     6 terms  

 

 
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

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PDB codes: 3ham 3hav
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Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG.
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PDB codes: 3g88 3g89 3g8a 3g8b
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Structure of the cytosine-cytosine mismatch in the thymidylate synthase mRNA binding site and analysis of its interaction with the aminoglycoside paromomycin.
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PDB code: 2rpt
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FRET enabled real time detection of RNA-small molecule binding.
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18824477 A.N.Petrov, A.Meskauskas, S.C.Roshwalb, and J.D.Dinman (2008).
Yeast ribosomal protein L10 helps coordinate tRNA movement through the large subunit.
  Nucleic Acids Res, 36, 6187-6198.  
18464793 A.V.Pisarev, V.G.Kolupaeva, M.M.Yusupov, C.U.Hellen, and T.V.Pestova (2008).
Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes.
  EMBO J, 27, 1609-1621.  
18060665 C.Foster, and W.S.Champney (2008).
Characterization of a 30S ribosomal subunit assembly intermediate found in Escherichia coli cells growing with neomycin or paromomycin.
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18510306 C.Guilbert, and T.L.James (2008).
Docking to RNA via root-mean-square-deviation-driven energy minimization with flexible ligands and flexible targets.
  J Chem Inf Model, 48, 1257-1268.  
17966131 C.H.Mak (2008).
RNA conformational sampling. I. Single-nucleotide loop closure.
  J Comput Chem, 29, 926-933.  
18058790 D.Balenci, F.Bernardi, L.Cellai, N.D'Amelio, E.Gaggelli, N.Gaggelli, E.Molteni, and G.Valensin (2008).
Effect of Cu(II) on the complex between kanamycin A and the bacterial ribosomal A site.
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18058789 D.W.Staple, V.Venditti, N.Niccolai, L.Elson-Schwab, Y.Tor, and S.E.Butcher (2008).
Guanidinoneomycin B recognition of an HIV-1 RNA helix.
  Chembiochem, 9, 93.
PDB code: 2juk
17987316 E.C.Böttger, and B.Springer (2008).
Tuberculosis: drug resistance, fitness, and strategies for global control.
  Eur J Pediatr, 167, 141-148.  
18768810 E.Roberts, A.Sethi, J.Montoya, C.R.Woese, and Z.Luthey-Schulten (2008).
Molecular signatures of ribosomal evolution.
  Proc Natl Acad Sci U S A, 105, 13953-13958.  
18003936 H.Fan-Minogue, and D.M.Bedwell (2008).
Eukaryotic ribosomal RNA determinants of aminoglycoside resistance and their role in translational fidelity.
  RNA, 14, 148-157.  
18844986 H.Grosjean, C.Gaspin, C.Marck, W.A.Decatur, and V.de Crécy-Lagard (2008).
RNomics and Modomics in the halophilic archaea Haloferax volcanii: identification of RNA modification genes.
  BMC Genomics, 9, 470.  
18084030 H.J.Haiser, F.V.Karginov, G.J.Hannon, and M.A.Elliot (2008).
Developmentally regulated cleavage of tRNAs in the bacterium Streptomyces coelicolor.
  Nucleic Acids Res, 36, 732-741.  
18468905 J.Heredia-Moya, and K.L.Kirk (2008).
Synthesis of beta-(S-methyl)thioaspartic acid and derivatives.
  Bioorg Med Chem, 16, 5908-5913.  
18346970 J.Kondo, and E.Westhof (2008).
The bacterial and mitochondrial ribosomal A-site molecular switches possess different conformational substates.
  Nucleic Acids Res, 36, 2654-2666.
PDB codes: 3bnl 3bnn 3bno 3bnp 3bnq 3bnr 3bns 3bnt
18973356 J.Romanowska, P.Setny, and J.Trylska (2008).
Molecular dynamics study of the ribosomal A-site.
  J Phys Chem B, 112, 15227-15243.  
18550838 J.W.Park, J.S.Hong, N.Parajuli, W.S.Jung, S.R.Park, S.K.Lim, J.K.Sohng, and Y.J.Yoon (2008).
Genetic dissection of the biosynthetic route to gentamicin A2 by heterologous expression of its minimal gene set.
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18310077 K.Fukui, M.Nishida, N.Nakagawa, R.Masui, and S.Kuramitsu (2008).
Bound nucleotide controls the endonuclease activity of mismatch repair enzyme MutL.
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18485067 L.E.Lancaster, A.Savelsbergh, C.Kleanthous, W.Wintermeyer, and M.V.Rodnina (2008).
Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes.
  Mol Microbiol, 69, 390-401.  
18355231 L.P.Thapa, T.J.Oh, K.Liou, and J.K.Sohng (2008).
Biosynthesis of spectinomycin: heterologous production of spectinomycin and spectinamine in an aminoglycoside-deficient host, Streptomyces venezuelae YJ003.
  J Appl Microbiol, 105, 300-308.  
18567815 M.A.Borovinskaya, S.Shoji, K.Fredrick, and J.H.Cate (2008).
Structural basis for hygromycin B inhibition of protein biosynthesis.
  RNA, 14, 1590-1599.
PDB codes: 3df1 3df2 3df3 3df4
19343095 M.Długosz, J.M.Antosiewicz, and J.Trylska (2008).
Association of aminoglycosidic antibiotics with the ribosomal A-site studied with Brownian dynamics.
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18174989 M.Hainrichson, I.Nudelman, and T.Baasov (2008).
Designer aminoglycosides: the race to develop improved antibiotics and compounds for the treatment of human genetic diseases.
  Org Biomol Chem, 6, 227-239.  
18187576 M.Simonović, and T.A.Steitz (2008).
Cross-crystal averaging reveals that the structure of the peptidyl-transferase center is the same in the 70S ribosome and the 50S subunit.
  Proc Natl Acad Sci U S A, 105, 500-505.