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Crystal structure of Thermatoga mritima ribosome recycling factor: A tRNA mimic

Selmer, Maria LU ; Al-Karadaghi, Salam LU ; Hirokawa, Go; Kaji, Akira and Liljas, Anders LU (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:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Science
volume
286
issue
5448
pages
2349 - 2352
publisher
The American Association for the Advancement of Science
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
2008-07-17 10:45:47
date last changed
2017-06-18 04:31:39
@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    = {The American Association for the Advancement of Science},
  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},
  volume       = {286},
  year         = {1999},
}