X-ray Crystal Structure Analysis of Ribosomal Protein S7.
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- HOSAKA Harumi
- Division of Biological Sciences, Graduate School of Science, Hokkaido University
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- TANAKA Isao
- Division of Biological Sciences, Graduate School of Science, Hokkaido University
Bibliographic Information
- Other Title
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- リボソームタンパク質S7のX線結晶構造解析
- 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
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Abstract
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.
Journal
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- Nihon Kessho Gakkaishi
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Nihon Kessho Gakkaishi 40 (5), 316-321, 1998
The Crystallographic Society of Japan
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Details 詳細情報について
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- CRID
- 1390001204086137984
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- NII Article ID
- 10002590973
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- NII Book ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL BIB ID
- 4596259
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed