Assignments of 1 H and 15 N resonances of the bacteriophage λ capsid stabilizing protein gpD

Content Provider	Semantic Scholar
Author	Iwaia, Hideo Forrerb, Patrik Plückthunb, Andreas Günterta, Peter
Copyright Year	2003
Abstract	The Escherichia coli bacteriophage λ virion is comprised of an icosahedral head and a long flexible non-contractile tail, and has been extensively studied as a model system for virus assembly (Hendrix et al., 1983; Dokland and Murialdo, 1993). Like all icosahedral dsDNA bacteriophages, the morphogenesis of bacteriophage λ proceeds through the assembly of an empty prohead, which is subsequently filled with DNA. The shell of the procapsid is composed mainly from gpE. DNA packaging is accompanied by expansion of the shell and binding of the 109 amino-acid protein gpD. The binding sites for gpD are created or exposed only after the prohead expands (Imber et al., 1980). gpD is not required for prohead assembly itself but is essential if a full-length genome is to be stably accommodated in the λ capsid. Thus, it is believed that gpD is necessary for stabilizing the capsid. In addition, Nand C-terminal fusion peptides and proteins of gpD have been used in λ phage display (Sternberg et al., 1995; Mikawa et al., 1996). The homo-trimeric structure of gpD in crystals has been determined and this structure is also present on the phage capsid, as observed by cryo-electron microscopy of empty capsids at 15 Å resolution (Yang et al., 2000). In the crystal structure, however, the functionally required N-terminal region is not defined. Interestingly, gpD exists stably as a monomer even at millimolar concentrations in solution in contrast with the crystal structure. The present NMR assignments will allow the detailed characterization of the ∗Present address: Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon S7N 5C9, Canada. ∗∗To whom correspondence should be addressed. E-mail: guentert@gsc.riken.go.jp N-terminal region and provide a basis for further studies of the interaction between gpD and the phage λ capsid, and hence, for the understanding of the virion assembly process.
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Resource Type	Article