Structure of the reovirus core at 3.6?Å resolution (original) (raw)
References
Fields,B. N. in Fields Virology (eds Fields, B. N., Knipe, D. M. & Howley, P. M.) 1553–1555 (Lippincott-Raven, Philadelphia, 1996). Google Scholar
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). Google Scholar
Grimes,J. M. et al. The atomic structure of the bluetongue virus core. Nature395, 470–478 ( 1998). ArticleADSCAS Google Scholar
Furuichi,Y., Muthukrishnan,S., Tomasz, J. & Shatkin,A. Mechanism and formation of reovirus mRNA 5′-terminal blocked and methylated sequence m7GpppGmpC. J. Biol. Chem.251, 5043–5053 ( 1976). CASPubMed Google Scholar
Earnshaw,W. C. & Harrison,S. C. DNA arrangement in isometric phage heads. Nature268, 598– 602 (1977). ArticleADSCAS Google Scholar
Dryden,K. A. et al. Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus. Virology245, 33–46 ( 1998). ArticleCAS Google Scholar
Gouet,P. et al. The highly ordered double-stranded RNA genome of bluetongue virus revealed by crystallography. Cell97, 481 –490 (1999). ArticleCAS Google Scholar
Hill,C. L. et al. The structure of cypovirus and the functional organization of dsRNA viruses. Nature Struct. Biol.6, 565 –568 (1999). ArticleCAS Google Scholar
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). ArticleCAS Google Scholar
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. Science256, 1783–1790 ( 1992). ArticleADSCAS Google Scholar
Stehle,T., Yan,Y., Benjamin,T. L. & Harrison,S. C. Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment. Nature369, 160–163 ( 1994). ArticleADSCAS Google Scholar
Liddington,R. C. et al. Structure of simian virus 40 at 3.8?Å resolution. Nature354, 278–284 (1991). ArticleADSCAS Google Scholar
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). CASPubMedPubMed Central Google Scholar
Moss,S. R. & Nuttall,P. A. Subcore- and core-like particles of Broadhaven virus (BRDV), a tick-bourne orbivirus, synthesized from baculovirus expressed VP2 and VP7, the major core proteins of BRVD. Virus Res.32, 401–407 ( 1994). ArticleCAS Google Scholar
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. Virology197, 726– 731 (1993). ArticleCAS Google Scholar
Mao,Z. & Joklik,W. K. Isolation and enzymatic characterization of protein λ2, the reovirus guanylyltransferase. Virology185, 377–386 ( 1991). ArticleCAS Google Scholar
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 l2. J. Biol. Chem.275, 2804–2810 (2000). ArticleCAS Google Scholar
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. Cell89, 545–553 (1997). Article Google Scholar
Schluckebier,G., O'Gara,M., Saenger,W. & Cheng,X. Universal catalytic domain structure of AdoMet-dependent methyltransferases. J. Mol. Biol.247, 16–20 ( 1995). ArticleCAS Google Scholar
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. Cell85, 247–256 (1996). ArticleCAS Google Scholar
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. USA96, 7149–7154 ( 1999). ArticleADSCAS Google Scholar
Wickner,S., Maurizi,M. R. & Gottesman, S. Posttranslational quality control: Folding, refolding, and degrading proteins. Science286, 1888 –1893 (1999). ArticleCAS Google Scholar
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. Cell14, 559– 568 (1978). ArticleCAS Google Scholar
Harvey,J. D., Bellamy,A. R., Earnshaw,W. C. & Schutt,C. Biophysical studies of reovirus type 3: iv low-angle x-ray diffraction studies. Virology112, 240–249 (1981). ArticleCAS Google Scholar
Harrison,S. C. Packaging of DNA into bacteriophage heads: a model. J. Mol. Biol.171, 577–580 ( 1983). ArticleCAS Google Scholar
Cerritelli,M. E. et al. Encapsidated conformations of bacteriophage T7 DNA. Cell91, 271–280 ( 1997). ArticleCAS Google Scholar
Booy,F. P. et al. Liquid crystalline, phage-like packing of encapsidated DNA in herpes simplex virus. Cell64, 1007– 1015 (1991). ArticleCAS Google Scholar
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). ArticleCAS Google Scholar
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). ArticleCAS Google Scholar
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. Structure4, 957– 967 (1996). ArticleCAS Google Scholar
Zhang,H. et al. Visualization of protein–RNA interactions in cytoplasmic polyhedrosis virus. J. Virol.73, 1624– 1629 (1999). CASPubMedPubMed Central Google Scholar
Prasad,B. V., Wang,G. J., Clerx,J. P. & Chiu,W. Three-dimensional structure of rotavirus. J. Mol. Biol.199, 269–275 (1988). ArticleCAS Google Scholar
Coombs,K. M., Fields,B. N. & Harrison, S. C. Crystallization of the reovirus type 3 Dearing core. J. Mol. Biol.215, 1–5 (1990). ArticleCAS Google Scholar
Otwinowski,Z. & Minor,W. in Macromolecular Crystallography A (eds Carter, C. W. & Sweet, R. M.) 307–326 (Academic, New York, 1997). Book Google Scholar
CCP4. The CCP4 suite: programs for X-ray crystallography. Acta Crystallogr. D50, 760–763 (1994). Article Google Scholar
Jones,T. A. in Molecular Replacement (eds Dodson, E. J., Gover, S. & Wolf, W.) 91–105 (SERC Daresbury Laboratory, Warrington, 1992). Google Scholar
Kleywegt,G. J. & Jones,T. A. in From First Map to Final Model (eds Bailey, S., Hubbard, R. & Waller, D.) 59–66 (SERC Daresbury Laboratory, Warrington, 1994). Google Scholar
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. A47, 110–119 (1991). Article Google Scholar
Brunger,A. T. et al. Crystallography & NMR System: a new software suite for macromolecular structure determination. Acta Crystallogr. D54, 905–921 (1998). ArticleCAS Google Scholar
Jacobsen,D. H., Hogle,J. M. & Filman, D. J. A pseudo-cell based approach to efficient crystallographic refinement of viruses. Acta Crystallogr. D52, 693–711 (1996). Article Google Scholar
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. Crystallogr.26, 283– 291 (1993). ArticleCAS Google Scholar
Carson,M. in Macromolecular Enzymology (eds Carter, C. W. Jr & Sweet, R. M.) 493–505 (Academic, New York, 1996). Google Scholar
Esnouf,R. M. An extensively modified version of Molscript that includes greatly enhanced coloring capabilities. J. Mol. Graphics15, 133–138 (1997). Google Scholar
Merrit,E. A. & Murphy,M. E. P. Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crsytallogr. D50, 869–873 (1994). Article Google Scholar
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). ArticleCAS Google Scholar
Harrison,S. J. et al. Mammalian reovirus L3 gene sequences and evidence for a distinct amino-terminal region of the lambda1 protein. Virology258, 54–64 (1999). ArticleCAS Google Scholar