HK97
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HK97 is a dsDNA lambdoid phage named for the site of its isolation (Hong Kong). It has a host range of E. coli and related bacteria. The capsid protein of HK97, gp5, cross-links upon maturation to form a concatenated chain-mail like structure.[1] The bacteriophage undergoes a maturation process upon DNA packaging during which it expands by nearly 5 nm and changes from spherically symmetrical to icosahedrally symmetrical.
The HK97 assembly pathway begins with self-assembly of the capsid protein, gp5, into pentamers and hexamers. A protease, gp4, cleaves gp5 at its N-terminus. Attachment of a portal protein, gp3, coupled with conformational changes leads to formation of a prohead or procapsid structure. Further conformational changes and crosslinking of gp5 monomers comprise further capsid maturation and lead to formation of a mature phage head.[citation needed]
[edit] References
- ^ The refined structure of a protein catenane, Journal of Molecular Biology, 12 December 2003
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