Summary for 3JD5
| Entry DOI | 10.2210/pdb3jd5/pdb |
| EMDB information | 5941 |
| Descriptor | 28S ribosomal RNA, mitochondial, 28S ribosomal protein S12, mitochondrial, 28S ribosomal protein S14, mitochondrial, ... (32 entities in total) |
| Functional Keywords | mitoribosome, mammalian 55s mitoribosome, protein synthesis, rna-protein complex, ribosome |
| Biological source | Bos taurus (bovine) More |
| Total number of polymer chains | 33 |
| Total formula weight | 1123253.92 |
| Authors | Kaushal, P.S.,Sharma, M.R.,Booth, T.M.,Haque, E.M.,Tung, C.S.,Sanbonmatsu, K.Y.,Spremulli, L.L.,Agrawal, R.K. (deposition date: 2016-04-08, release date: 2016-07-13, Last modification date: 2025-06-11) |
| Primary citation | Kaushal, P.S.,Sharma, M.R.,Booth, T.M.,Haque, E.M.,Tung, C.S.,Sanbonmatsu, K.Y.,Spremulli, L.L.,Agrawal, R.K. Cryo-EM structure of the small subunit of the mammalian mitochondrial ribosome. Proc.Natl.Acad.Sci.USA, 111:7284-7289, 2014 Cited by PubMed Abstract: The mammalian mitochondrial ribosomes (mitoribosomes) are responsible for synthesizing 13 membrane proteins that form essential components of the complexes involved in oxidative phosphorylation or ATP generation for the eukaryotic cell. The mammalian 55S mitoribosome contains significantly smaller rRNAs and a large mass of mitochondrial ribosomal proteins (MRPs), including large mito-specific amino acid extensions and insertions in MRPs that are homologous to bacterial ribosomal proteins and an additional 35 mito-specific MRPs. Here we present the cryo-EM structure analysis of the small (28S) subunit (SSU) of the 55S mitoribosome. We find that the mito-specific extensions in homologous MRPs generally are involved in inter-MRP contacts and in contacts with mito-specific MRPs, suggesting a stepwise evolution of the current architecture of the mitoribosome. Although most of the mito-specific MRPs and extensions of homologous MRPs are situated on the peripheral regions, they also contribute significantly to the formation of linings of the mRNA and tRNA paths, suggesting a tailor-made structural organization of the mito-SSU for the recruitment of mito-specific mRNAs, most of which do not possess a 5' leader sequence. In addition, docking of previously published coordinates of the large (39S) subunit (LSU) into the cryo-EM map of the 55S mitoribosome reveals that mito-specific MRPs of both the SSU and LSU are involved directly in the formation of six of the 15 intersubunit bridges. PubMed: 24799711DOI: 10.1073/pnas.1401657111 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7 Å) |
Structure validation
Download full validation report
