PMID:12244297
| Citation |
Tung, CS, Joseph, S and Sanbonmatsu, KY (2002) All-atom homology model of the Escherichia coli 30S ribosomal subunit. Nat. Struct. Biol. 9:750-5 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1038/nsb841 |
| Keywords |
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 |
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