Journal
SCIENCE
Volume 348, Issue 6230, Pages 95-98Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaa1193
Keywords
-
Categories
Funding
- UK MRC [MC_U105184332, MC_UP_A025_1013]
- Wellcome Trust [WT096570]
- Agouron Institute
- Jeantet Foundation
- MRC [MC_UP_A025_1013]
- Medical Research Council [MC_UP_A025_1013, MC_U105184332] Funding Source: researchfish
- Wellcome Trust [096570/Z/11/Z] Funding Source: researchfish
- MRC [MC_U105184332, MC_UP_A025_1013] Funding Source: UKRI
Ask authors/readers for more resources
The highly divergent ribosomes of human mitochondria (mitoribosomes) synthesize 13 essential proteins of oxidative phosphorylation complexes. We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by means of single-particle electron cryogenic microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three ribosomal RNA molecules. The head domain of the small subunit, particularly the messenger (mRNA) channel, is highly remodeled. Many intersubunit bridges are specific to the mitoribosome, which adopts conformations involving ratcheting or rolling of the small subunit that are distinct from those seen in bacteria or eukaryotes. An intrinsic guanosine triphosphatase mediates a contact between the head and central protuberance. The structure provides a reference for analysis of mutations that cause severe pathologies and for future drug design.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available