リボソームタンパク質Ｓ７のＸ線結晶構造解析

• 保坂 晴美

  北海道大学大学院理学研究科生物科学専攻

• 田中 勲

  北海道大学大学院理学研究科生物科学専攻

書誌事項

タイトル別名

• X-ray Crystal Structure Analysis of Ribosomal Protein S7.
• リボソームタンパクシツ S7 ノ Xセン ケッショウ コウゾウ カイセキ

抄録

The structure of ribosomal protein S7 from Bacillus stearothermophilus has been solved at 2.5 Å resolution by multiwavelength anomalous diffraction method using selenomethionyl-substituted proteins. The molecule consists of a helical hydrophobic core domain and a β-ribbon arm extending from the hydrophobic core. The helical core domain is composed of a pair of entangled helix-turn-helix motifs; the fold of the core is similar to that of a DNA architectural factor. Highly conserved basic and aromatic residues are clustered on one face of the S7 molecule and create a 16S rRNA contact surface. The molecular structure of S7, together with the results of previous cross-linking experiments, suggests how this ribosomal protein binds to the 3' major domain of 16S rRNA and mediates the folding of 16S rRNA to create the ribosome decoding center.

収録刊行物

• 日本結晶学会誌

  日本結晶学会誌 40 (5), 316-321, 1998

  日本結晶学会

詳細情報

• CRID: 1390001204086137984
• NII論文ID: 10002590973
• NII書誌ID: AN00188364
• DOI: 10.5940/jcrsj.40.316
• ISSN: 18845576
• ISSN: 03694585
• NDL書誌ID: 4596259
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I4596259
• 本文言語コード: ja
• データソース種別:
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• 抄録ライセンスフラグ: 使用不可