The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22.

Article Details

Citation

Gabashvili IS, Gregory ST, Valle M, Grassucci R, Worbs M, Wahl MC, Dahlberg AE, Frank J

The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22.

Mol Cell. 2001 Jul;8(1):181-8.

PubMed ID
11511371 [ View in PubMed
]
Abstract

Variations in the inner ribosomal landscape determining the topology of nascent protein transport have been studied by three-dimensional cryo-electron microscopy of erythromycin-resistant Escherichia coli 70S ribosomes. Significant differences in the mouth of the 50S subunit tunnel system visualized in the present study support a simple steric-hindrance explanation for the action of the drug. Examination of ribosomes in different functional states suggests that opening and closing of the main tunnel are dynamic features of the large subunit, possibly accompanied by changes in the L7/L12 stalk region. The existence and dynamic behavior of side tunnels suggest that ribosomal proteins L4 and L22 might be involved in the regulation of a multiple exit system facilitating cotranslational processing (or folding or directing) of nascent proteins.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
50S ribosomal protein L4P60723Details