Skip to main content
Biophysical Journal logoLink to Biophysical Journal
. 1980 Nov;32(2):677–695. doi: 10.1016/S0006-3495(80)85009-0

A computer model for the 30S ribosome subunit.

I D Kuntz, G M Crippen
PMCID: PMC1327231  PMID: 7020786

Abstract

We describe a computer-generated model for the locations of the 21 proteins of the 30S subunit of the E. coli ribosome. The model uses a new method of incorporating experimental measurements based on a mathematical technique called distance geometry. In this paper, we use data from two sources: immunoelectron microscopy and neutron-scattering studies. The data are generally self-consistent and lead to a set of relatively well-defined structures in which individual protein coordinates differ by approximately 20 A from one structure to another. Two important features of this calculation are the use of extended proteins rather than just the centers of mass, and the ability to confine the protein locations within an arbitrary boundary surface so that only solutions with an approximate 30S "shape" are permitted.

Full text

PDF
677

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bollen A., Cedergren R. J., Sankoff D., Lapalme G. Spatial configuration of ribosomal proteins: a computer-generated model of the 30S subunit. Biochem Biophys Res Commun. 1974 Aug 5;59(3):1069–1078. doi: 10.1016/s0006-291x(74)80088-4. [DOI] [PubMed] [Google Scholar]
  2. Brimacombe R., Stöffler G., Wittmann H. G. Ribosome structure. Annu Rev Biochem. 1978;47:217–249. doi: 10.1146/annurev.bi.47.070178.001245. [DOI] [PubMed] [Google Scholar]
  3. Changchien L. M., Craven G. R. Proximity relationships among the 30 S ribosomal proteins during assembly in vitro. J Mol Biol. 1977 Jun 15;113(1):103–122. doi: 10.1016/0022-2836(77)90043-2. [DOI] [PubMed] [Google Scholar]
  4. Cornick G. G., Kretsinger R. H. The 30 S subunit of the Escherichia coli ribosome. Topographical model of its component proteins. Biochim Biophys Acta. 1977 Feb 3;474(3):398–410. doi: 10.1016/0005-2787(77)90269-6. [DOI] [PubMed] [Google Scholar]
  5. Crippen G. M. Distance constraints on macromolecular conformation. Int J Pept Protein Res. 1979 Mar;13(3):320–326. doi: 10.1111/j.1399-3011.1979.tb01886.x. [DOI] [PubMed] [Google Scholar]
  6. Engelman D. M., Moore P. B., Schoenborn B. P. Neutron scattering measurements of separation and shape of proteins in 30S ribosomal subunit of Escherichia coli: S2-S5, S5-S8, S3-S7. Proc Natl Acad Sci U S A. 1975 Oct;72(10):3888–3892. doi: 10.1073/pnas.72.10.3888. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Gaffney P. T., Craven G. Use of computerized multidimensional scaling to compare immunoelectron microscopy data with protein near-neighbor information: application to the 30S ribosome from Escherichia coli. Proc Natl Acad Sci U S A. 1978 Jul;75(7):3128–3132. doi: 10.1073/pnas.75.7.3128. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Langer J. A., Engelman D. M., Moore P. B. Neutron-scattering studies of the ribosome of Escherichia coli: a provisional map of the locations of proteins S3, S4, S5, S7, S8 and S9 in the 30 S subunit. J Mol Biol. 1978 Mar 15;119(4):463–485. doi: 10.1016/0022-2836(78)90197-3. [DOI] [PubMed] [Google Scholar]
  9. Moore P. B., Langer J. A., Schoenborn B. P., Engelman D. M. Triangulation of proteins in the 30 S ribosomal subunit of Exherichia coli. J Mol Biol. 1977 May 15;112(2):199–227. doi: 10.1016/s0022-2836(77)80139-3. [DOI] [PubMed] [Google Scholar]
  10. Schindler D. G., Langer J. A., Engelman D. M., Moore P. B. Positions of proteins S10, S11 and S12 in the 30 S ribosomal subunit of Escherichia coli. J Mol Biol. 1979 Nov 5;134(3):595–620. doi: 10.1016/0022-2836(79)90369-3. [DOI] [PubMed] [Google Scholar]
  11. Ycas M., Goel N. S., Jacobsen J. W. On the computation of the tertiary structure of globular proteins. J Theor Biol. 1978 Jun 6;72(3):443–457. doi: 10.1016/0022-5193(78)90311-9. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES