Structure of the reovirus core at 3.6 Å resolution

Nature

Volumn 404, Issue 6781, 2000, Pages 960-967

  Reinisch, Karin M ^a   Nibert, Max L ^c   Harrison, Stephen C ^a,b  

^a HARVARD UNIVERSITY   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^c UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS RNA;

ARTICLE; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; REOVIRUS; RNA ANALYSIS; RNA CAPPING; VIRUS MORPHOLOGY; X RAY CRYSTALLOGRAPHY;

CAPSID; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; PROTEIN CONFORMATION; REOVIRIDAE; RNA CAPS; RNA, DOUBLE-STRANDED; RNA, VIRAL;

EID: 0034720237     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35010041     Document Type: Article

References (46)

1. Fields, B. N. in Fields Virology (eds Fields, B. N., Knipe, D. M. & Howley, P. M.) 1553-1555 (Lippincott-Raven, Philadelphia, 1996).
2. Nibert, M. L., Schiff, L. A. & Fields, B. N. in Fields Virology (eds Fields, B. N., Knipe, D. M. & Howley, P. M.) 1557-1596 (Lippincott-Raven, Philadelphia, 1996).
3. Grimes, J. M. et al. The atomic structure of the bluetongue virus core. Nature 395, 470-478 (1998).
4. mpC. J. Biol. Chem. 251, 5043-5053 (1976).
5. Earnshaw, W. C. & Harrison, S. C. DNA arrangement in isometric phage heads. Nature 268, 598-602 (1977).
6. Dryden, K. A. et al. Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus. Virology 245, 33-46 (1998).
7. Gouet, P. et al. The highly ordered double-stranded RNA genome of bluetongue virus revealed by crystallography. Cell 97, 481-490 (1999).
8. Hill, C. L. et al. The structure of cypovirus and the functional organization of dsRNA viruses. Nature Struct. Biol. 6, 565-568 (1999).
9. Dryden, K. A. et al. Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction. J. Cell Biol. 122, 1023-1041 (1993).
10. Kohlstaedt, L. A., Wang, J., Friedman, J. M., Rice, P. A. & Steitz, T. A. Crystal structure of 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 256, 1783-1790 (1992).
11. Stehle, T., Yan, Y., Benjamin, T. L. & Harrison, S. C. Structure of murine polyomavirvis complexed with an oligosaccharide receptor fragment. Nature 369, 160-163 (1994).
12. Liddington, R. C. et al. Structure of simian virus 40 at 3.8 Å resolution. Nature 354, 278-284 (1991).
13. Labbe, M., Charpilienne, A., Crawford, S. E., Estes, M. K. & Cohen, J. Expression of rotavirus VP2 produces empty corelike particles. J. Virol. 65, 2946-2952 (1991).
14. Moss, S. R. & Nuttall, P. A. Subcore- and core-like particles of Broadhaven virus (BRDV), a tickbourne orbivirus, synthesized from baculovirus expressed VP2 and VP7, the major core proteins of BHVD. Virus Res. 32, 401-407 (1994).
15. Xu, P., Miller, S. & Joklik, W. K. Generation of reovirus core-like particles in cells infected with hybrid vaccinia viruses that express genome segments L1, L2, L3, and S2. Virology 197, 726-731 (1993).
16. Mao, Z. & Joklik, W. K. Isolation and enzymatic characterization of protein λ2, the reovirus guanylyltransferase. Virology 185, 377-386 (1991).
17. Luongo, C. L., Reinisch, K. M., Harrison, S. C. & Nibert, M. L. Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein 12. J. Biol. Chem. 275, 2804-2810 (2000).
18. Håkansson, K., Doherty, A. J., Shuman, S. & Wigley, D. B. X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes. Cell 89, 545-553 (1997).
19. Schluckebier, G., O'Gara, M., Saenger, W. & Cheng, X. Universal catalytic domain structure of AdoMet-dependent methyltransferases. J. Mol. Biol. 247, 16-20 (1995).
20. Hodel, A. E., Gershon, P. D., Shi, X. & Quiocho, F. A. The 1.85 Å structure of the vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends. Cell 85, 247-256 (1996).
21. Hu, G., Gershon, P. D., Hodel, A. E. & Quiocho, F. A. mRNA cap recognition: dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains. Proc. Natl Acad. Sci. USA 96, 7149-7154 (1999).
22. Wickner, S., Maurizi, M. R. & Gottesman, S. Posttranslational quality control: Folding, refolding, and degrading proteins. Science 286, 1888-1893 (1999).
23. Earnshaw, W. C., King, J., Harrison, S. C. & Eiserling, F. A. The structural organization of DNA packaged within the heads of T4 wild-type, isometric and giant bacteriophages. Cell 14, 559-568 (1978).
24. Harvey, J. D., Bellamy, A. R., Earnshaw, W. C. & Schutt, C. Biophysical studies of reovirus type 3: iv low-angle x-ray diffraction studies. Virology 112, 240-249 (1981).
25. Harrison, S. C. Packaging of DNA into bacttriophage heads: a model. J. Mol. Biol. 171, 577-580 (1983).
26. Cerritelli, M. E. et al. Encapsidated conformations of bacteriophage T7 DNA. Cell 91, 271-280 (1997).
27. Booy, F. P. et al. Liquid crystalline, phage-like packing of encapsidated DNA in herpes simplex virus. Cell 64, 1007-1015 (1991).
28. Butcher, S. J., Dokland, T., Ojala, P. M., Bamford, D. H. & Fuller, S. D. Intermediates in the assembly pathway of the double-stranded RNA virus φ6, EMBO J. 16, 4477-4487 (1997).
29. Cheng, R. H. et al. Fungal virus capsids, cytoplasmic compartments for the replication of double-stranded RNA, formed as icosahedral shells of asymmetric Gag dimers. J. Mol. Biol. 244, 255-258 (1994).
30. Shaw, A. L., Samal, S. K., Subramanian, K. & Prasad, B. V. V. The structure of aquareovirus shows how the different geometries of the two layers of capsid are reconciled to provide symmetrical interactions and stabilization. Structure 4, 957-967 (1996).
31. Zhang, H. et al. Visualization of protein-RNA interactions in cytoplasmic polyhedrosis virus. J. Virol. 73, 1624-1629 (1999).
32. Prasad, B. V., Wang, G. J., Clerx, J. P. & Chiu, W. Three-dimensional structure of rotavirus. J. Mol. Biol. 199, 269-275 (1988).
33. Coombs, K. M., Fields, B. N. & Harrison, S. C. Crystallization of the reovirus type 3 Dearing core. J. Mol. Biol. 215, 1-5 (1990).
34. Otwinowski, Z. & Minor, W. in Macromolecular Crystallography A (eds Carter, C. W. & Sweet, R. M.) 307-326 (Academic, New York, 1997).
35. CCP4. The CCP4 suite: programs for X-ray crystallography. Acta Crystallogr. D 50, 760-763 (1994).
36. Jones, T. A. in Molecular Replacement (eds Dodson, E. J., Gover, S. & Wolf, W.) 91-105 (SERC Daresbury Laboratory, Warrington, 1992).
37. Kleywegt, G. J. & Jones, T. A. in From First Map to Final Model (eds Bailey, S., Hubbard, R. & Walter, D.) 59-66 (SERC Daresbury Laboratory, Warrington, 1994).
38. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjelgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
39. Brunger, A. T. et al Crystallography & NMR System: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
40. Jacobsen, D. H., Hogle, J. M. & Filman, D. J. A pseudo-cell based approach to efficient crystaltographic refinement of viruses. Acta Crystallogr. D 52, 693-711 (1996).
41. Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crytallogr. 26, 283-291 (1993).
42. Carson, M. in Macromolecular Enzymology (eds Carter, C. W. Jr & Sweet, R. M.) 493-505 (Academic, New York, 1996).
43. Esnouf, R. M. An extensively modified version of Molscript that includes greatly enhanced coloring capabilities. J. Mol. Graphics 15, 133-138 (1997).
44. Merrit, E. A. & Murphy, M. E. P. Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crsytaltogr. D 50, 869-873 (1994).
45. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296 (1991).
46. Harrison, S. J. et al. Mammalian reovirus L3 gene sequences and evidence for a distinct amino-terminal region of the lambda1 protein. Virology 258, 54-64 (1999).