1CWP
STRUCTURES OF THE NATIVE AND SWOLLEN FORMS OF COWPEA CHLOROTIC MOTTLE VIRUS DETERMINED BY X-RAY CRYSTALLOGRAPHY AND CRYO-ELECTRON MICROSCOPY
1CWP の概要
| エントリーDOI | 10.2210/pdb1cwp/pdb |
| 分子名称 | RNA (5'-R(*AP*UP*AP*U)-3'), RNA (5'-R(*AP*U)-3'), Coat protein (3 entities in total) |
| 機能のキーワード | bromovirus, icosahedral virus, virus-rna complex, virus/rna |
| 由来する生物種 | Cowpea chlorotic mottle virus |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 64050.74 |
| 構造登録者 | Speir, J.A.,Johnson, J.E.,Munshi, S.,Wang, G.,Timothy, S.,Baker, T.S. (登録日: 1995-05-22, 公開日: 1995-05-22, 最終更新日: 2024-02-14) |
| 主引用文献 | Speir, J.A.,Munshi, S.,Wang, G.,Baker, T.S.,Johnson, J.E. Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy. Structure, 3:63-77, 1995 Cited by PubMed Abstract: RNA-protein interactions stabilize many viruses and also the nucleoprotein cores of enveloped animal viruses (e.g. retroviruses). The nucleoprotein particles are frequently pleomorphic and generally unstable due to the lack of strong protein-protein interactions in their capsids. Principles governing their structures are unknown because crystals of such nucleoprotein particles that diffract to high resolution have not previously been produced. Cowpea chlorotic mottle virions (CCMV) are typical of particles stabilized by RNA-protein interactions and it has been found that crystals that diffract beyond 4.5 A resolution are difficult to grow. However, we report here the purification of CCMV with an exceptionally mild procedure and the growth of crystals that diffract X-rays to 3.2 A resolution. PubMed: 7743132DOI: 10.1016/S0969-2126(01)00135-6 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.2 Å) |
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