Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex
During the translation cycle, a cognate deacylated tRNA can only move together with the codon into the E site. We here present the first structure of a cognate tRNA bound to the ribosomal E site resulting from translocation by EF-G, in which an entire L1 stalk (L1 protein and L1 rRNA) interacts wi...
| Main Authors: | , , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
| Published: |
2013
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| Subjects: | |
| Online Access: | https://hdl.handle.net/10356/96532 http://hdl.handle.net/10220/9877 |
| _version_ | 1811691411662176256 |
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| author | Feng, Shu Chen, Yun Gao, Yong-Gui |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Feng, Shu Chen, Yun Gao, Yong-Gui |
| author_sort | Feng, Shu |
| collection | NTU |
| description | During the translation cycle, a cognate deacylated tRNA can only move together with the codon into the E site. We here
present the first structure of a cognate tRNA bound to the ribosomal E site resulting from translocation by EF-G, in which an
entire L1 stalk (L1 protein and L1 rRNA) interacts with E-site tRNA (E-tRNA), representing an authentic ribosome elongation
complex. Our results revealed that the Watson-Crick base pairing is formed at the first and second codon-anticodon
positions in the E site in the ribosome elongation complex, whereas the codon-anticodon interaction in the third position is
indirect. Analysis of the observed conformations of mRNA and E-tRNA suggests that the ribosome intrinsically has the
potential to form codon-anticodon interaction in the E site, independently of the mRNA configuration. We also present a
detailed description of the biologically relevant position of the entire L1 stalk and its interacting cognate E-tRNA, which
provides a better understanding of the structural basis for translation elongation. Furthermore, to gain insight into
translocation, we report the positioning of protein L6 contacting EF-G, as well as the conformational change of the Cterminal
tail of protein S13 in the decoding center. |
| first_indexed | 2024-10-01T06:19:28Z |
| format | Journal Article |
| id | ntu-10356/96532 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T06:19:28Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | ntu-10356/965322023-02-28T16:55:58Z Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex Feng, Shu Chen, Yun Gao, Yong-Gui School of Biological Sciences DRNTU::Science::Biological sciences::Microbiology During the translation cycle, a cognate deacylated tRNA can only move together with the codon into the E site. We here present the first structure of a cognate tRNA bound to the ribosomal E site resulting from translocation by EF-G, in which an entire L1 stalk (L1 protein and L1 rRNA) interacts with E-site tRNA (E-tRNA), representing an authentic ribosome elongation complex. Our results revealed that the Watson-Crick base pairing is formed at the first and second codon-anticodon positions in the E site in the ribosome elongation complex, whereas the codon-anticodon interaction in the third position is indirect. Analysis of the observed conformations of mRNA and E-tRNA suggests that the ribosome intrinsically has the potential to form codon-anticodon interaction in the E site, independently of the mRNA configuration. We also present a detailed description of the biologically relevant position of the entire L1 stalk and its interacting cognate E-tRNA, which provides a better understanding of the structural basis for translation elongation. Furthermore, to gain insight into translocation, we report the positioning of protein L6 contacting EF-G, as well as the conformational change of the Cterminal tail of protein S13 in the decoding center. Published version 2013-05-03T07:01:01Z 2019-12-06T19:31:58Z 2013-05-03T07:01:01Z 2019-12-06T19:31:58Z 2013 2013 Journal Article Feng, S., Chen, Y., & Gao, Y. G. (2013). Crystal Structure of 70S Ribosome with Both Cognate tRNAs in the E and P Sites Representing an Authentic Elongation Complex. PLoS ONE, 8(3). 1932-6203 https://hdl.handle.net/10356/96532 http://hdl.handle.net/10220/9877 10.1371/journal.pone.0058829 23527033 en PLoS ONE © 2013 The Author(s). application/pdf |
| spellingShingle | DRNTU::Science::Biological sciences::Microbiology Feng, Shu Chen, Yun Gao, Yong-Gui Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex |
| title | Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex |
| title_full | Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex |
| title_fullStr | Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex |
| title_full_unstemmed | Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex |
| title_short | Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex |
| title_sort | crystal structure of 70s ribosome with both cognate trnas in the e and p sites representing an authentic elongation complex |
| topic | DRNTU::Science::Biological sciences::Microbiology |
| url | https://hdl.handle.net/10356/96532 http://hdl.handle.net/10220/9877 |
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