The Refined Crystal Structure of Cowpea Mosaic Virus at 2.8 Å Resolution
| Autor: | John E. Johnson, R. Usha, Tianwei Lin, Tim Schmidt, Cynthia V. Stauffacher, Zhongguo Chen, Jin-Bi Dai |
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| Jazyk: | angličtina |
| Předmět: |
Models
Molecular Picornavirus biology Protein Conformation viruses Comovirus Molecular Sequence Data Cowpea mosaic virus Mineralogy Antigen-Antibody Complex Crystal structure Antibodies Viral Crystallography X-Ray biology.organism_classification Nucleoprotein Viral Proteins Crystallography Capsid Plant virus Virology RNA Viral Cubic form Molecular replacement Amino Acid Sequence |
| Zdroj: | Virology. (1):20-34 |
| ISSN: | 0042-6822 |
| DOI: | 10.1006/viro.1999.0038 |
| Popis: | Comoviruses are a group of plant viruses in the picornavirus superfamily. The type member of comoviruses, cowpea mosaic virus (CPMV), was crystallized in the cubic space group I23, a = 317 A and the hexagonal space group P6(1)22, a = 451 A, c = 1038 A. Structures of three closely similar nucleoprotein particles were determined in the cubic form. The roughly 300-A capsid was similar to the picornavirus capsid displaying a pseudo T = 3 (P = 3) surface lattice. The three beta-sandwich domains adopt two orientations, one with the long axis radial and the other two with the long axes tangential in reference to the capsid sphere. T = 3 viruses display one or the other of these two orientations. The CPMV capsid was permeable to cesium ions, leading to a disturbance of the beta-annulus inside a channel-like structure, suggesting an ion channel. The hexagonal crystal form diffracted X rays to 3 A resolution, despite the large unit cell. The large ( approximately 200 A) solvent channels in the lattice allow exchange of CPMV cognate Fab fragments. As an initial step in the structure determination of the CPMV/Fab complex, the P6(1)22 crystal structure was solved by molecular replacement with the CPMV model determined in the cubic cell. |
| Databáze: | OpenAIRE |
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