van Raaij, Mark J. and Schoehn, Guy and Jaquinod, Michel and Ashman, Keith and Burda, Martin R. and Miller, Stefan (2001) Identification and crystallisation of a heat- and protease-stable fragment of the bacteriophage T4 short tail fibre. BIOLOGICAL CHEMISTRY, 382 (7). pp. 1049-1055. ISSN 1431-6730
Full text not available from this repository.Abstract
Irreversible binding of T-even bacteriophages to Escherichia coli is mediated by the short tail fibres, which serve as inextensible stays during DNA injection. Short tail fibres are exceptionally stable elongated trimers of gene product 12 (gp12), a 56 kDa protein. The N-terminal region of gp12 is important for phage attachment, the central region forms a long shaft, while a C-terminal globular region is implicated in binding to the bacterial lipopolysaccharide core. When gp12 was treated with stoichiometric amounts of trypsin or chymotrypsin at 37 degreesC, an N-terminally shortened fragment of 52 kDa resulted. If the protein was incubated at 56 degreesC before trypsin treatment at 37 degreesC, we obtained a stable trimeric fragment of 3 x 33 kDa lacking residues from both the N- and C-termini. Apparently, the protein unfolds partially at 56 degreesC, thereby exposing protease-sensitive sites in the C-terminal region and extra sites in the N-terminal region. Well-diffracting crystals of this fragment could be grown. Our results indicate that gp12 carries a stable central region, consisting of the C-terminal part of the shaft and the attached N-terminal half of the globular region. Implications for structure determination of the gp12 protein and its folding are discussed.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | TAILSPIKE ENDORHAMNOSIDASE; CRYSTAL-STRUCTURE; ADENOVIRUS FIBER; BINDING DOMAIN; PROTEINS; bacteriophage T4 adhesin; crystallisation; electron microscopy; heat and protease stability; short tail fibre; X-ray diffraction |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 21 Dec 2021 09:28 |
| Last Modified: | 21 Dec 2021 09:28 |
| URI: | https://pred.uni-regensburg.de/id/eprint/41272 |
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