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6NF8

Structure of human mitochondrial translation initiation factor 3 bound to the small ribosomal subunit -Class I

Summary for 6NF8
Entry DOI10.2210/pdb6nf8/pdb
Related3JD5
EMDB information9362
Descriptor28S ribosomal RNA, mitochondria, 28S ribosomal protein S27, mitochondrial, 28S ribosomal protein S34, mitochondrial, ... (32 entities in total)
Functional Keywordsmitochondrial translation initiation factor 3, ribosomal protein
Biological sourceBos taurus (Bovine)
More
Total number of polymer chains32
Total formula weight1143408.54
Authors
Sharma, M.,Koripella, R.,Agrawal, R. (deposition date: 2018-12-19, release date: 2019-02-27, Last modification date: 2024-10-23)
Primary citationKoripella, 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: 30677741
DOI: 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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