Identification and crystallisation of a heat- and protease-stable fragment of the bacteriophage T4 short tail fibre

van Raaij, Mark J., Schoehn, Guy, Jaquinod, Michel, Ashman, Keith, 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: 1049-1055. doi:10.1515/BC.2001.131

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Author van Raaij, Mark J.
Schoehn, Guy
Jaquinod, Michel
Ashman, Keith
Burda, Martin R.
Miller, Stefan
Title Identification and crystallisation of a heat- and protease-stable fragment of the bacteriophage T4 short tail fibre
Journal name Biological Chemistry   Check publisher's open access policy
ISSN 1431-6730
1437-4315
Publication date 2001-07
Sub-type Article (original research)
DOI 10.1515/BC.2001.131
Open Access Status File (Publisher version)
Volume 382
Issue 7
Start page 1049
End page 1055
Total pages 7
Place of publication Berlin, Germany
Publisher Walter de Gruyter
Language eng
Abstract Irreversible binding of Teven 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 Nterminal region of gp12 is important for phage attachment, the central region forms a long shaft, while a Cterminal globular region is implicated in binding to the bacterial lipopolysaccharide core. When gp12 was treated with stoichiometric amounts of trypsin or chymotrypsin at 37 C, an Nterminally shortened fragment of 52 kDa resulted. If the protein was incubated at 56 C before trypsin treatment at 37 C, we obtained a stable trimeric fragment of 3 33 kDa lacking residues from both the N and Ctermini. Apparently, the protein unfolds partially at 56 C, thereby exposing proteasesensitive sites in the Cterminal region and extra sites in the Nterminal region. Welldiffracting crystals of this fragment could be grown. Our results indicate that gp12 carries a stable central region, consisting of the Cterminal part of the shaft and the attached Nterminal half of the globular region. Implications for structure determination of the gp12 protein and its folding are discussed.
Keyword Bacteriophage T4 adhesin
Crystallisation
Electron microscopy
Heat and protease stability
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: UQ Centre for Clinical Research Publications
 
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