1ohf
From Proteopedia
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THE REFINED STRUCTURE OF NUDAURELIA CAPENSIS OMEGA VIRUS
Overview
Large-scale reorganization of protein interactions characterizes many, biological processes, yet few systems are accessible to biophysical, studies that display this property. The capsid protein of Nudaurelia, capensis omega Virus (NomegaV) has previously been characterized in two, dramatically different T = 4 quasi-equivalent assembly states when, expressed as virus-like particles (VLPs) in a baculovirus system. The, procapsid (pH 7), is round, porous, and approximately 450 A in diameter., It converts, in vitro, to the capsid form at pH 5 and the capsid is sealed, shut, shaped like an icosahedron, has a maximum diameter of 410 A and, undergoes an autocatalytic cleavage at residue 570. Residues 571-644, the, gamma peptide, remain associated with the particle and are partially, ordered. ... [(full description)]
About this Structure
1OHF is a [Single protein] structure of sequence from [Nudaurelia capensis omega virus] with MG as [ligand]. Full crystallographic information is available from [OCA].
Reference
The refined structure of Nudaurelia capensis omega virus reveals control elements for a T = 4 capsid maturation., Helgstrand C, Munshi S, Johnson JE, Liljas L, Virology. 2004 Jan 5;318(1):192-203. PMID:14972547
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