Tail tip proteins related to bacteriophage λ gpL coordinate an iron-sulfur cluster.

ABSTRACT: The assembly of long non-contractile phage tails begins with the formation of the tail tip complex (TTC). TTCs are multi-functional protein structures that mediate host cell adsorption and genome injection. The TTC of phage λ is assembled from multiple copies of eight different proteins, including gpL. Purified preparations of gpL and several homologues all displayed a distinct reddish color, suggesting the binding of iron by these proteins. Further characterization of the gpL homologue from phage N15, which was most amenable to in vitro analyses, showed that it contains two domains. The C-terminal domain was demonstrated to coordinate an iron-sulfur cluster, providing the first example of a viral structural protein binding to this type of metal group. We characterized the iron-sulfur clus

SUBMITTER: Tam W 

PROVIDER: S-EPMC4061613 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature