A crevice adjoining the ribosome tunnel: hints for cotranslational folding.
RNA protection experiments and the crystal structure of a complex of the large ribosomal subunit from the eubacterium Deinococcus radiodurans with rapamycin, a polyketide compound resembling macrolides and ketolides, showed that rapamycin binds to a crevice located at the boundaries of the nascent protein exit tunnel, near its entrance. At this location rapamycin cannot occlude the ribosome exit tunnel, consistent with its failure to act as a ribosomal antibiotic drug. In accord with recent biochemical data, this crevice may play a role in facilitating local cotranslational folding of nascent chains, in particular for transmembrane proteins.
Amit
Maya
M
Department of Structural Biology, The Weizmann Institute, 76100 Rehovot, Israel.
Berisio
Rita
R
Baram
David
D
Harms
Joerg
J
Bashan
Anat
A
Yonath
Ada
A
D001483:Base Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D034301:Deinococcus / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D009690:Nucleic Acid Conformation; D014176:Protein Biosynthesis / Q000187:drug effects; D017510:Protein Folding; D012338:RNA, Ribosomal, 23S / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism*; D020123:Sirolimus / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology
D012338:RNA, Ribosomal, 23S; D020123:Sirolimus