Abstract:
:Tet(O) belongs to a class of ribosomal protection proteins that mediate tetracycline resistance. It is a G protein that shows significant sequence similarity to elongation factor EF-G. Here we present a cryo-electron microscopic reconstruction, at 16 A resolution, of its complex with the E. coli 70S ribosome. Tet(O) was bound in the presence of a noncleavable GTP analog to programmed ribosomal complexes carrying fMet-tRNA in the P site. Tet(O) is directly visible as a mass close to the A-site region, similar in shape and binding position to EF-G. However, there are important differences. One of them is the different location of the tip of domain IV, which in the Tet(O) case, does not overlap with the ribosomal A site but is directly adjacent to the primary tetracycline binding site. Our findings give insights into the mechanism of tetracycline resistance.
journal_name
Mol Celljournal_title
Molecular cellauthors
Spahn CM,Blaha G,Agrawal RK,Penczek P,Grassucci RA,Trieber CA,Connell SR,Taylor DE,Nierhaus KH,Frank Jdoi
10.1016/s1097-2765(01)00238-6subject
Has Abstractpub_date
2001-05-01 00:00:00pages
1037-45issue
5eissn
1097-2765issn
1097-4164pii
S1097-2765(01)00238-6journal_volume
7pub_type
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