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2DOG

Solution structure of the N-terminal domain of RimM from Thermus thermophilus HB8

2DOG の概要
エントリーDOI10.2210/pdb2dog/pdb
NMR情報BMRB: 10138
分子名称Probable 16S rRNA-processing protein rimM (1 entity in total)
機能のキーワードbeta barrel, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, structural genomics, unknown function
由来する生物種Thermus thermophilus
細胞内の位置Cytoplasm (By similarity): Q5SJH5
タンパク質・核酸の鎖数1
化学式量合計9493.97
構造登録者
主引用文献Suzuki, S.,Tatsuguchi, A.,Matsumoto, E.,Kawazoe, M.,Kaminishi, T.,Shirouzu, M.,Muto, Y.,Takemoto, C.,Yokoyama, S.
Structural characterization of the ribosome maturation protein, RimM
J.Bacteriol., 189:6397-6406, 2007
Cited by
PubMed Abstract: The RimM protein has been implicated in the maturation of the 30S ribosomal subunit. It binds to ribosomal protein S19, located in the head domain of the 30S subunit. Multiple sequence alignments predicted that RimM possesses two domains in its N- and C-terminal regions. In the present study, we have produced Thermus thermophilus RimM in both the full-length form (162 residues) and its N-terminal fragment, spanning residues 1 to 85, as soluble proteins in Escherichia coli and have performed structural analyses by nuclear magnetic resonance spectroscopy. Residues 1 to 80 of the RimM protein fold into a single structural domain adopting a six-stranded beta-barrel fold. On the other hand, the C-terminal region of RimM (residues 81 to 162) is partly folded in solution. Analyses of 1H-15N heteronuclear single quantum correlation spectra revealed that a wide range of residues in the C-terminal region, as well as the residues in the vicinity of a hydrophobic patch in the N-terminal domain, were dramatically affected upon complex formation with ribosomal protein S19.
PubMed: 17616598
DOI: 10.1128/JB.00024-07
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2dog
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2025-05-14に公開中

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