Crystal structure of the 30s ribosome

Details Crystal structure of the 30s ribosome Crystal structure of the 30s ribosome

2005-08-02

2005-08-02

Marschel, Ardin H. (Department: 1631)

Data processing: measuring, calibrating, or testing

Measurement system in a specific environment

Chemical analysis

C702S019000, C702S010000, C702S010000

Reexamination Certificate

active

06925394

ABSTRACT:
The invention provides an X-ray crystal structure of the 30S ribosome, obtained fromThermus thermophilus30S subunit, having a tetragonal space group P41212 with unit cell dimensions of a=401.4±4.0 Å, b=401.4±4.0 Å, c=175.9±5.0 Å. An advantageous feature of the structure is that it diffracts beyond 3 Å resolution. The invention also provides a crystal of 30S having the three dimensional atomic coordinates of the 30S ribosome, the coordinates being provided in Tables 1A and 1B. The data may be used for the rational design and modelling of inhibitors for the 30S ribosome, which have potential use as antibiotics.

REFERENCES:
Jan Drenth, Principles of Protein X-ray Crystallography, 1995, Springer-Verlag, p. 16.
News Focus, Science, Nov. 1, 2002, vol. 298, pp. 948-950.
Bhuyan, B. K, et al. (1961). “Pactamycin, A New Antitumor Antibiotic: Discovery and Biological Properties,”Antimicrob Agents Chemother184-190.
Böck, A. et al. (1979). “Ribosomal Ambiguity (Ram) Mutations Facilitate Dihydrostreptomycin Binding to Ribosomes,”FEBS Letters104(2):317-321.
Brink, M. F. et al. (1994). “Spectinomycin Interacts Specifically with the Residues G1064 and C1192 in 16S rRNA, Thereby Poteentially Freeaing This Molecule Into an Inactive Conformation,”Nucleic Acids Res22(3):325-331.
Brodersen et al. “the Structural Basis for th e Action of the Antibiotics Tetracycline, Pactamycin and Hygromycin B on the 30S Ribosomal Subunit,”Cell103:1143-1154 (2000).
Brown, C. M. et al. (1993). “Two Regions of the Escherichia Coli 16S Ribosomal RNA Are Inportant for Decoding Stop Signals in Polypeptide Chain Termination,”Nucleic Acids Res21(9):2109-2115.
Cabanas, M. J. et al. (1978). “Inhibition of Ribosomal Translocation by Aminoglycoside Antibiotics,”Biochem Biophys Res Commun83(3):991-997.
Carter et al. (2000). “Functional Insights from the Structure of the 30S Ribosomal Subunit and its Interactions with Antibiotics,”Nature407:340-348.
Chopra, I. et al. (1992). “Tetracyclines, Molecular and Clinical Aspects,”J. Antimicrob Chemother29:245-277.
Clemons, Jr., W. et al. (1999). “Structure of a Bacterial 30S Ribosomal Subunit at 5.5 Å Resolution,”Nature400:833-840.
Clemons, Jr., W. et al. (2001). “Crystal Structure of the 30S Ribosomal Subunit from Thermus Thermophilus: Purification, Crystallization and Structure Determination,”J. Mol. Biol. 310:827-843.
Cohen, L. B. et al. (1969). “Inhibition by Pactamycin of the Initiation of Protein Synthesis. Effect on the 30S Ribosomal Subunit,”Biochemistry8(4):1327-1335.
De la Fortelle, E. and Bricogne, G. (1997). “Maximum-Likelihood Heavy-Atom Parameter Refinement for Multiple Isomorphous Replacement and Multiwavelength Anamalous Diffraction Mehods,” InMethods in Enzymology, eds. Carter, C. W., Jr. Sweet, R. M, Academic Press, New York, 1997, pp. 472-493.
Donner, D. and Kurland, C. G. (1972). “Changes in the Primary Structure of a Mutationally Altered Ribosomal Protein S4 ofEscherichia coli,” Mol Gen Genet115:49-53.
Egebjerg, J. and Garrett, R. A. (1991). “Binding Sites of the Antibiotics Pactamycin and Celesticetin on Ribosomal RNAs,”Biochimie73:1145-1149.
Eustice, D. C and Wilhelm, J. M. (1984). “Mechanisms of Action of Aminoglycoside Antibiotics in Eucaryotic Protein Synthesis,”Antimicrob Agents Chemother26(1):53-60.
Eustice, D. C. and Wilhelm, J. M. (1984). “Fidelity of the Eukaryotic Codon-Anticodon Interaction: Interference by Aminoglycoside Antibiotics,”Biochemistry23:1462-1467.
Fourmy, D. et al. (1996). “Structure of the A Site ofEscherichia coli16S Ribosomal RNA Complexed with an Aminoglycoside Antibiotic,”Science274:1367-1371.
Funatsu, G. and Wittmann, H. G. (1972). “Location of Amino-Acid Replacements in Protein S12 Isolated fromEscherichia coliMutants Resistant to Streptomycin,”J. Mol Biol68:547-550.
Funatsu, G. et al. (1972). “Ribosomal Proteins. XXXI. Comparative Studies on Altered Proteins S4 of SicEscherichia coliRevertants from Streptomycin Dependence,”Mol Gen Genet115:131-149.
Geigenmüller, U. and Nierhaus, K. H. (1986). “Tetracycline Can Inhibit tRNA Binding to the Ribosomal P Site as Well as to the A Site,”Eur. J. Biochem161:723-726.
Gonzales, A. et al. (1978). “Studies on The Mode of Action of Hygromycin B, An Inhibitor of Translocation in Eukaryotes,”Biochim Biophys Acta521:459-469.
Gravel, M. et al. (1987). “Cross-Linking of Streptomychin to the 16S Ribosomal RNA ofEscherichia coli,” Biochemistry26:6227-6232.
Hope, H. et al. (1989). “Cyrocrystallography of Ribosomal Particles,”Acta Cryst. B45:190-199.
Ito, T. and Wittmann, H. G. (1973). “Amino Acid Replacements in Proteins S5 and S12 of TwoEscherichia coliRevertants from Streptomycin Dependence to Independence,”Mol. Gen. Genet, 127:19-32.
Kolesnikov, I. V. et al. (1996). “Tetracyclines Induce Changes in Accessibility of Ribosomal Proteins to Proteases,”Biochimie78:868-873.
Harland, C. G. et al. (1996). “Limitations of Translational Accuracy” Chapter 65In Escherichia Coli andSalmonella, Cellular and Molecular Biology, Second Edition, vol. 2, Neidhart,F. C. et al., eds. American Society for Microbiology Press, Washington D.C., pp. 979-1004. Includes Table of Contents.
Leclerc, D. et al. (1991). “Mutations in the 915 Region ofEscherichia coli16S Ribosomal RNA Reduce the Binding of Streptomycin to the Ribosome,”Nucleic Acids Res. 19(14):3973-3977.
Manavathu, E. K. et al. (1990). “Molecular Studies on the Mechanism of Tetracycline Resistance Mediated by Tet(O),”Antimicrob Agents Chemother34(1):71-77.
Mann, R. L. and Bromer, W. W. (1958). “Isolation of a Second Antibiotic from Streptomyces Hygroscopicus,”J. Am. Chem. Soc. 80:2714-2716.
Melancon, P. et al. (1984). “Cross-Lining of Streptomycin to the 30S Subunit ofEscherichia coliwith Phenyldiglyoxal,”Biochemistry23:6697-6703.
Melancon, P. et al. (1988). “A Mutation in the 530 Loop ofEscherichia coli16S Ribosomal RNA Causes Resistance to Streptomycin,”Nucleic Acids Res16(2):9631-9339.
Moazed, D. and Noller, H. F. (1987). “Interaction of Antibiotics with Functional Sites in 16S Ribosomal RNA,”Nature337:389-394.
Montadon, P. E. et al. (1985). “Streptomycin-Resistance of Euglena Gracilis Chloroplasts: Identification of a Point Mutation in the 16S rRNA Gene in an Invariant Position,”Nucleic Acids Res. 13(12):4299-4310.
Montandon, P. E. et al. (1986). “E. coliRibosomes with a C912 to U Base Change in the 16s rRNA are Streptomycin Resistant,”EMBO J. 5(3):3705-3708.
Mueller, F. and Brimacombe, R. (1997). “A New Model for the Three-Dimensional Folding ofEscherichia coli16 S Ribosomal RNA. I. Fitting the RNA to a 3D Electron Microscopic Map at 20 Å,”J. Mol. Biol. 271:524-544.
Oehler, R. et al. (1997). “Interaction of Tetracycline with RNA: Photoincorporation into Ribosomal RNA ofEscherichia coli,” Nucleic Acids Res25(6):1219-1224.
Ogle, J. M. et al. (2001). “Recognition of Cognate Transfer RNA by the 30S Ribosomal Subunit,”Science292:897-902.
Pape, T. et al. (2000). “Conformational Switch in the Decoding Region of 16s rRNA During Aminoacyl-tRNA Selection on the Ribosome,”Nat. Struct. Biol. 7(2):104-107.
Pinard, R. et al. (1993). “The 5′ Proximal Helix of 16S rRNA is Involved in the Binding of Streptomycin to the Ribosome”,FASEB J. 7:173-176.
Pioletti, M. et al. (2001). “Crystal Structures of Complexes of the Small Ribosomal Subunit with Tetracycline, Edeine and IF3,”EMBO Journal20(8):1829-1839.
Powers, T. and Noller, H. F. (1991). “A Functional Pseudoknot in 16S Ribosomal RNA,”EMBO J. 10:2203-2214.
Ross, J. I. et al. (1998). “16

Affiliated with

Also associated with

Rating

Crystal structure of the 30s ribosome does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Crystal structure of the 30s ribosome, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Crystal structure of the 30s ribosome will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3476145