Abstract:
:Ribosomes are translational machineries that catalyse protein synthesis. Ribosome structures from various species are known at the atomic level, but obtaining the structure of the human ribosome has remained a challenge; efforts to address this would be highly relevant with regard to human diseases. Here we report the near-atomic structure of the human ribosome derived from high-resolution single-particle cryo-electron microscopy and atomic model building. The structure has an average resolution of 3.6 Å, reaching 2.9 Å resolution in the most stable regions. It provides unprecedented insights into ribosomal RNA entities and amino acid side chains, notably of the transfer RNA binding sites and specific molecular interactions with the exit site tRNA. It reveals atomic details of the subunit interface, which is seen to remodel strongly upon rotational movements of the ribosomal subunits. Furthermore, the structure paves the way for analysing antibiotic side effects and diseases associated with deregulated protein synthesis.
journal_name
Naturejournal_title
Natureauthors
Khatter H,Myasnikov AG,Natchiar SK,Klaholz BPdoi
10.1038/nature14427subject
Has Abstractpub_date
2015-04-30 00:00:00pages
640-5issue
7549eissn
0028-0836issn
1476-4687pii
nature14427journal_volume
520pub_type
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