6NF8
Structure of human mitochondrial translation initiation factor 3 bound to the small ribosomal subunit -Class I
Summary for 6NF8
Entry DOI | 10.2210/pdb6nf8/pdb |
Related | 3JD5 |
EMDB information | 9362 |
Descriptor | 28S ribosomal RNA, mitochondria, 28S ribosomal protein S27, mitochondrial, 28S ribosomal protein S34, mitochondrial, ... (32 entities in total) |
Functional Keywords | mitochondrial translation initiation factor 3, ribosomal protein |
Biological source | Bos taurus (Bovine) More |
Total number of polymer chains | 32 |
Total formula weight | 1143408.54 |
Authors | Sharma, M.,Koripella, R.,Agrawal, R. (deposition date: 2018-12-19, release date: 2019-02-27, Last modification date: 2024-10-23) |
Primary citation | Koripella, R.K.,Sharma, M.R.,Haque, M.E.,Risteff, P.,Spremulli, L.L.,Agrawal, R.K. Structure of Human Mitochondrial Translation Initiation Factor 3 Bound to the Small Ribosomal Subunit. iScience, 12:76-86, 2019 Cited by PubMed Abstract: The human mitochondrial translational initiation factor 3 (IF3) carries mitochondrial-specific amino acid extensions at both its N and C termini (N- and C-terminal extensions [NTE and CTE, respectively]), when compared with its eubacterial counterpart. Here we present 3.3- to 3.5-Å-resolution cryoelectron microscopic structures of the mammalian 28S mitoribosomal subunit in complex with human IF3. Unique contacts observed between the 28S subunit and N-terminal domain of IF3 explain its unusually high affinity for the 28S subunit, whereas the position of the mito-specific NTE suggests NTE's role in binding of initiator tRNA to the 28S subunit. The location of the C-terminal domain (CTD) clarifies its anti-association activity, whereas the orientation of the mito-specific CTE provides a mechanistic explanation for its role in destabilizing initiator tRNA in the absence of mRNA. Furthermore, our structure hints at a possible role of the CTD in recruiting leaderless mRNAs for translation initiation. Our findings highlight unique features of IF3 in mitochondrial translation initiation. PubMed: 30677741DOI: 10.1016/j.isci.2018.12.030 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.48 Å) |
Structure validation
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