Highly Discriminatory Binding of Capsid-Cementing Proteins in Bacteriophage L
نویسندگان
چکیده
منابع مشابه
Maturation dynamics of bacteriophage HK97 capsid.
Maturation of the bacteriophage HK97 capsid requires a large conformational change of the virus capsid. Experimental studies have identified several intermediates along this maturation pathway. To gain insights into the molecular mechanisms of capsid maturation, we examined the fluctuation dynamics of the procapsid and mature capsid using a residue-level computational approach. The most coopera...
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Coat proteins (CPs) of all plant viruses have an early function in disassembly of parental virus and a late function in assembly of progeny virus. Depending on the virus, however, CPs may play a role in many steps of the infection cycle in between these early and late functions. It has been shown that CPs can play a role in translation of viral RNA, targeting of the viral genome to its site of ...
متن کاملDifferentiation of Two Abortive Mechanisms by Using Monoclonal Antibodies Directed toward Lactococcal Bacteriophage Capsid Proteins.
Monoclonal antibodies were used to monitor the accumulation of the major capsid protein of the lactococcal small isometric bacteriophage u136 (P335 species) over the course of a one-step growth curve. A sandwich enzyme-linked immunosorbent assay was then used to distinguish two abortive phage resistance mechanisms, Hsp and Prf. Capsid protein production of u136 was almost totally inhibited by t...
متن کاملAnalysis of Human Papillomavirus Capsid Proteins: Insights into Capsid Assembly
Papillomaviruses (PVs) are double stranded (ds)-DNA viruses (~8-kbp), which infect mucosal and cutaneous epithelial cells from various mammalian species, causing tumors in both epithelial cell-types [22, 48-50, 64, 65]. During the early-phase of an HPV infection; the genome is maintained within the basal epithelium establishing the primary infection, while during the latephase, the capsid prote...
متن کاملTopologically linked protein rings in the bacteriophage HK97 capsid.
The crystal structure of the double-stranded DNA bacteriophage HK97 mature empty capsid was determined at 3.6 angstrom resolution. The 660 angstrom diameter icosahedral particle contains 420 subunits with a new fold. The final capsid maturation step is an autocatalytic reaction that creates 420 isopeptide bonds between proteins. Each subunit is joined to two of its neighbors by ligation of the ...
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ژورنال
عنوان ژورنال: Structure
سال: 2006
ISSN: 0969-2126
DOI: 10.1016/j.str.2006.03.010