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-Structure paper
タイトル | The crystal structure of the bacterial chaperonin GroEL at 2.8 A. |
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ジャーナル・号・ページ | Nature, Vol. 371, Issue 6498, Page 578-586, Year 1994 |
掲載日 | 1994年10月13日 |
著者 | K Braig / Z Otwinowski / R Hegde / D C Boisvert / A Joachimiak / A L Horwich / P B Sigler / |
PubMed 要旨 | The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry. The subunits ...The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry. The subunits consist of three domains: a large equatorial domain that forms the foundation of the assembly at its waist and holds the rings together; a large loosely structured apical domain that forms the ends of the cylinder; and a small slender intermediate domain that connects the two, creating side windows. The three-dimensional structure places most of the mutationally defined functional sites on the channel walls and its outward invaginations, and at the ends of the cylinder. |
リンク | Nature / PubMed:7935790 |
手法 | X線回折 |
解像度 | 2.8 Å |
構造データ | PDB-1grl: |
由来 |
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キーワード | CHAPERONIN |