Crystal structure of Thermatoga mritima ribosome recycling factor: A tRNA mimic
(1999) In Science 286(5448). p.2349-2352- Abstract
- Ribosome recycling factor (RRF), together with elongation factor G (EF-G), catalyzes recycling of ribosomes after one round of protein synthesis. The crystal structure of RRF was determined at 2.55 angstrom resolution. The protein has an unusual fold where domain I is a long three-helix bundle and domain II is a three-layer β/α/β sandwich. The molecule superimposes almost perfectly with a transfer RNA (tRNA) except that the amino acid-binding 3′ end is missing. The mimicry suggests that RRF interacts with the posttermination ribosomal complex in a similar manner to a tRNA, leading to disassembly of the complex. The structural arrangement of this mimicry is entirely different from that of other cases of less pronounced mimicry of tRNA so... (More)
- Ribosome recycling factor (RRF), together with elongation factor G (EF-G), catalyzes recycling of ribosomes after one round of protein synthesis. The crystal structure of RRF was determined at 2.55 angstrom resolution. The protein has an unusual fold where domain I is a long three-helix bundle and domain II is a three-layer β/α/β sandwich. The molecule superimposes almost perfectly with a transfer RNA (tRNA) except that the amino acid-binding 3′ end is missing. The mimicry suggests that RRF interacts with the posttermination ribosomal complex in a similar manner to a tRNA, leading to disassembly of the complex. The structural arrangement of this mimicry is entirely different from that of other cases of less pronounced mimicry of tRNA so far described. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/948632
- author
- Selmer, Maria LU ; Al-Karadaghi, Salam LU ; Hirokawa, Go ; Kaji, Akira and Liljas, Anders LU
- organization
- publishing date
- 1999
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Science
- volume
- 286
- issue
- 5448
- pages
- 2349 - 2352
- publisher
- American Association for the Advancement of Science (AAAS)
- external identifiers
-
- scopus:0033579365
- ISSN
- 1095-9203
- DOI
- 10.1126/science.286.5448.2349
- language
- English
- LU publication?
- yes
- id
- 9b47491d-92ec-484a-9a6a-a017d583b18c (old id 948632)
- alternative location
- http://www.jstor.org/stable/2899763
- date added to LUP
- 2016-04-01 16:38:06
- date last changed
- 2022-01-28 21:01:25
@article{9b47491d-92ec-484a-9a6a-a017d583b18c, abstract = {{Ribosome recycling factor (RRF), together with elongation factor G (EF-G), catalyzes recycling of ribosomes after one round of protein synthesis. The crystal structure of RRF was determined at 2.55 angstrom resolution. The protein has an unusual fold where domain I is a long three-helix bundle and domain II is a three-layer β/α/β sandwich. The molecule superimposes almost perfectly with a transfer RNA (tRNA) except that the amino acid-binding 3′ end is missing. The mimicry suggests that RRF interacts with the posttermination ribosomal complex in a similar manner to a tRNA, leading to disassembly of the complex. The structural arrangement of this mimicry is entirely different from that of other cases of less pronounced mimicry of tRNA so far described.}}, author = {{Selmer, Maria and Al-Karadaghi, Salam and Hirokawa, Go and Kaji, Akira and Liljas, Anders}}, issn = {{1095-9203}}, language = {{eng}}, number = {{5448}}, pages = {{2349--2352}}, publisher = {{American Association for the Advancement of Science (AAAS)}}, series = {{Science}}, title = {{Crystal structure of Thermatoga mritima ribosome recycling factor: A tRNA mimic}}, url = {{http://dx.doi.org/10.1126/science.286.5448.2349}}, doi = {{10.1126/science.286.5448.2349}}, volume = {{286}}, year = {{1999}}, }