Journal
SCIENCE
Volume 289, Issue 5487, Pages 2129-2133Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.289.5487.2129
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Funding
- NIAID NIH HHS [R01 AI040101, AI40101] Funding Source: Medline
- NIGMS NIH HHS [GM47795, R01 GM047795] Funding Source: Medline
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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 side-chain Lysine 169 to asparagine 356. This generates 12 pentameric and 60 hexameric rings of covalently joined subunits that loop through each other, creating protein chainmail: topologically linked protein catenanes arranged with icosahedral symmetry. Catenanes have not been previously observed in proteins and provide a stabilization mechanism for the very thin HK97 capsid.
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