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

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Tung CS, Joseph S, Sanbonmatsu KY

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

Nat Struct Biol. 2002 Oct;9(10):750-5.

PubMed ID
12244297 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
30S ribosomal protein S4P0A7V8Details
30S ribosomal protein S9P0A7X3Details
30S ribosomal protein S10P0A7R5Details
30S ribosomal protein S12P0A7S3Details
30S ribosomal protein S14P0AG59Details
30S ribosomal protein S13P0A7S9Details
30S ribosomal protein S19P0A7U3Details
30S ribosomal protein S3P0A7V3Details
30S ribosomal protein S8P0A7W7Details
30S ribosomal protein S7P02359Details