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1FEU

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN TL5, ONE OF THE CTC FAMILY PROTEINS, COMPLEXED WITH A FRAGMENT OF 5S RRNA.

1FEU の概要
エントリーDOI10.2210/pdb1feu/pdb
分子名称19 NT FRAGMENT OF 5S RRNA, 21 NT FRAGMENT OF 5S RRNA, 50S RIBOSOMAL PROTEIN L25, ... (6 entities in total)
機能のキーワードgeneral stress protein ctc, 5s rrna-protein complex, cadmium ions, ribosome
由来する生物種Thermus thermophilus
タンパク質・核酸の鎖数6
化学式量合計74373.42
構造登録者
主引用文献Fedorov, R.,Meshcheryakov, V.,Gongadze, G.,Fomenkova, N.,Nevskaya, N.,Selmer, M.,Laurberg, M.,Kristensen, O.,Al-Karadaghi, S.,Liljas, A.,Garber, M.,Nikonov, S.
Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins.
Acta Crystallogr.,Sect.D, 57:968-976, 2001
Cited by
PubMed 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 A 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 beta-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. Cd(2+) 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.
PubMed: 11418764
DOI: 10.1107/S0907444901006291
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.3 Å)
構造検証レポート
Validation report summary of 1feu
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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