English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Irreversible binding of Teven bacteriophages toEscherichia coli is mediated by the short tail fibres, which serve asinextensible stays during DNA injection. Short tail fibres are exceptionallystable elongated trimers of gene product 12 (gp12), a 56 kDa protein. TheNterminal region of gp12 is important for phage attachment, the central regionforms a long shaft, while a Cterminal globular region is implicated in bindingto the bacterial lipopolysaccharide core. When gp12 was treated withstoichiometric amounts of trypsin or chymotrypsin at 37 C, an Nterminallyshortened fragment of 52 kDa resulted. If the protein was incubated at 56 Cbefore trypsin treatment at 37 C, we obtained a stable trimeric fragment of 333 kDa lacking residues from both the N and Ctermini. Apparently, the proteinunfolds partially at 56 C, thereby exposing proteasesensitive sites in theCterminal region and extra sites in the Nterminal region. Welldiffractingcrystals of this fragment could be grown. Our results indicate that gp12carries a stable central region, consisting of the Cterminal part of the shaftand the attached Nterminal half of the globular region. Implications forstructure determination of the gp12 protein and its folding are discussed.

Identification and Crystallisation of a Heat- and Protease-Stable Fragment of the Bacteriophage T4 Short Tail Fibre