HK97 maturation studied by crystallography and H/2H exchange reveals the structural basis for exothermic particle transitions.

ABSTRACT: HK97 is an exceptionally amenable system for characterizing major conformational changes associated with capsid maturation in double-stranded DNA bacteriophage. HK97 undergoes a capsid expansion of approximately 20%, accompanied by major subunit rearrangements during genome packaging. A previous 3.44-A-resolution crystal structure of the mature capsid Head II and cryo-electron microscopy studies of other intermediate expansion forms of HK97 suggested that, primarily, rigid-body movements facilitated the maturation process. We recently reported a 3.65-A-resolution structure of the preexpanded particle form Prohead II (P-II) and found that the capsid subunits undergo significant refolding and twisting of the tertiary structure to accommodate expansion. The P-II study focused on major twistin

SUBMITTER: Gertsman I 

PROVIDER: S-EPMC2855905 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature