All-atom homology model of the Escherichia coli 30S ribosomal subunit

Nat Struct Biol. 2002 Oct;9(10):750-5. doi: 10.1038/nsb841.

Abstract

Understanding the structural basis of ribosomal function requires close comparison between biochemical and structural data. Although a large amount of biochemical data are available for the Escherichia coli ribosome, the structure has not been solved to atomic resolution. Using a new RNA homology procedure, we have modeled the all-atom structure of the E. coli 30S ribosomal subunit. We find that the tertiary structure of the ribosome core, including the A-, P- and E-sites, is highly conserved. The hypervariable regions in our structure, which differ from the structure of the 30S ribosomal subunit from Thermus thermophilus, are consistent with the cryo-EM map of the E. coli ribosome.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Base Sequence
  • Conserved Sequence
  • Escherichia coli / chemistry*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism
  • Models, Molecular
  • Protein Conformation
  • RNA, Ribosomal, 16S / chemistry
  • RNA, Ribosomal, 16S / metabolism
  • Ribosomal Proteins / chemistry*
  • Ribosomal Proteins / metabolism
  • Ribosomes / chemistry*
  • Ribosomes / metabolism
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Thermus thermophilus / genetics

Substances

  • Escherichia coli Proteins
  • RNA, Ribosomal, 16S
  • Ribosomal Proteins

Associated data

  • PDB/1M5G