Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins
(2001) In Acta Crystallographica. Section D: Biological Crystallography D57(7). p.968-976- Abstract
- The crystal structure of Thermus thermophilus ribosomal protein TL5 in complex with a fragment of Escherichia coli 5S rRNA has been determined at 2.3 Å resolution. The protein consists of two domains. The structure of the N-terminal domain is close to the structure of E. coli ribosomal protein L25, but the C-terminal domain represents a new fold composed of seven -strands connected by long loops. TL5 binds to the RNA through its N-terminal domain, whereas the C-terminal domain is not included in this interaction. Cd2+ ions, the presence of which improved the crystal quality significantly, bind only to the protein component of the complex and stabilize the protein molecule itself and the interactions between the two molecules in the... (More)
- The crystal structure of Thermus thermophilus ribosomal protein TL5 in complex with a fragment of Escherichia coli 5S rRNA has been determined at 2.3 Å resolution. The protein consists of two domains. The structure of the N-terminal domain is close to the structure of E. coli ribosomal protein L25, but the C-terminal domain represents a new fold composed of seven -strands connected by long loops. TL5 binds to the RNA through its N-terminal domain, whereas the C-terminal domain is not included in this interaction. Cd2+ ions, the presence of which improved the crystal quality significantly, bind only to the protein component of the complex and stabilize the protein molecule itself and the interactions between the two molecules in the asymmetric unit of the crystal. The TL5 sequence reveals homology to the so-called general stress protein CTC. The hydrophobic cores which stabilize both TL5 domains are highly conserved in CTC proteins. Thus, all CTC proteins may fold with a topology close to that of TL5. (Less)
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https://lup.lub.lu.se/record/948781
- author
- organization
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- general stress protein CTC, protein-RNA complex, cadmium ions
- in
- Acta Crystallographica. Section D: Biological Crystallography
- volume
- D57
- issue
- 7
- pages
- 968 - 976
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:14344278877
- ISSN
- 1399-0047
- language
- English
- LU publication?
- yes
- id
- 5c6def91-6403-4fd9-9678-7d267885992d (old id 948781)
- alternative location
- http://www.blackwell-synergy.com/doi/abs/10.1107/S0907444901006291
- date added to LUP
- 2016-04-01 15:19:09
- date last changed
- 2022-02-27 06:25:45
@article{5c6def91-6403-4fd9-9678-7d267885992d,
abstract = {{The crystal structure of Thermus thermophilus ribosomal protein TL5 in complex with a fragment of Escherichia coli 5S rRNA has been determined at 2.3 Å resolution. The protein consists of two domains. The structure of the N-terminal domain is close to the structure of E. coli ribosomal protein L25, but the C-terminal domain represents a new fold composed of seven -strands connected by long loops. TL5 binds to the RNA through its N-terminal domain, whereas the C-terminal domain is not included in this interaction. Cd2+ ions, the presence of which improved the crystal quality significantly, bind only to the protein component of the complex and stabilize the protein molecule itself and the interactions between the two molecules in the asymmetric unit of the crystal. The TL5 sequence reveals homology to the so-called general stress protein CTC. The hydrophobic cores which stabilize both TL5 domains are highly conserved in CTC proteins. Thus, all CTC proteins may fold with a topology close to that of TL5.}},
author = {{Fedorov, R V and Meshcheryakov, V A and Gongadze, G M and Fomenkova, N P and Nevskaya N A, N A and Selmer, Maria and Laurberg, Martin and Kristensen, Ole and Al-Karadaghi, Salam and Liljas, Anders and Garber, Marina and Nikonov, S}},
issn = {{1399-0047}},
keywords = {{general stress protein CTC; protein-RNA complex; cadmium ions}},
language = {{eng}},
number = {{7}},
pages = {{968--976}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Acta Crystallographica. Section D: Biological Crystallography}},
title = {{Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins}},
url = {{http://www.blackwell-synergy.com/doi/abs/10.1107/S0907444901006291}},
volume = {{D57}},
year = {{2001}},
}