Unknown

Dataset Information

0

Structure of the yeast mitochondrial large ribosomal subunit.


ABSTRACT: Mitochondria have specialized ribosomes that have diverged from their bacterial and cytoplasmic counterparts. We have solved the structure of the yeast mitoribosomal large subunit using single-particle cryo-electron microscopy. The resolution of 3.2 angstroms enabled a nearly complete atomic model to be built de novo and refined, including 39 proteins, 13 of which are unique to mitochondria, as well as expansion segments of mitoribosomal RNA. The structure reveals a new exit tunnel path and architecture, unique elements of the E site, and a putative membrane docking site.

SUBMITTER: Amunts A 

PROVIDER: S-EPMC4046073 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structure of the yeast mitochondrial large ribosomal subunit.

Amunts Alexey A   Brown Alan A   Bai Xiao-Chen XC   Llácer Jose L JL   Hussain Tanweer T   Emsley Paul P   Long Fei F   Murshudov Garib G   Scheres Sjors H W SHW   Ramakrishnan V V  

Science (New York, N.Y.) 20140301 6178


Mitochondria have specialized ribosomes that have diverged from their bacterial and cytoplasmic counterparts. We have solved the structure of the yeast mitoribosomal large subunit using single-particle cryo-electron microscopy. The resolution of 3.2 angstroms enabled a nearly complete atomic model to be built de novo and refined, including 39 proteins, 13 of which are unique to mitochondria, as well as expansion segments of mitoribosomal RNA. The structure reveals a new exit tunnel path and arch  ...[more]

Similar Datasets

2017-04-01 | GSE97276 | GEO
| S-EPMC2788216 | biostudies-literature
| S-EPMC4246062 | biostudies-literature
| S-EPMC2577338 | biostudies-literature
| S-EPMC2996981 | biostudies-literature
| S-EPMC4671574 | biostudies-literature
| S-EPMC2806038 | biostudies-literature
| S-EPMC3564531 | biostudies-literature
| S-EPMC102430 | biostudies-literature
| S-EPMC29789 | biostudies-literature