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https://hdl.handle.net/2440/3034
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dc.contributor.author | Freiberg, A. | - |
dc.contributor.author | Morona, R. | - |
dc.contributor.author | Van Den Bosch, L. | - |
dc.contributor.author | Jung, C. | - |
dc.contributor.author | Behlke, J. | - |
dc.contributor.author | Carlin, N. | - |
dc.contributor.author | Seckler, R. | - |
dc.contributor.author | Baxa, U. | - |
dc.date.issued | 2003 | - |
dc.identifier.citation | Journal of Biological Chemistry, 2003; 278(3):1542-1548 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.issn | 1083-351X | - |
dc.identifier.uri | http://hdl.handle.net/2440/3034 | - |
dc.description.abstract | Bacteriophage Sf6 tailspike protein is functionally equivalent to the well characterized tailspike of Salmonella phage P22, mediating attachment of the viral particle to host cell-surface polysaccharide. However, there is significant sequence similarity between the two 70-kDa polypeptides only in the N-terminal putative capsid-binding domains. The major, central part of P22 tailspike protein, which forms a parallel -helix and is responsible for saccharide binding and hydrolysis, lacks detectable sequence homology to the Sf6 protein. After recombinant expression in Escherichia coli as a soluble protein, the Sf6 protein was purified to homogeneity. As shown by circular dichroism and Fourier transform infrared spectroscopy, the secondary structure contents of Sf6 and P22 tailspike proteins are very similar. Both tailspikes are thermostable homotrimers and resist denaturation by SDS at room temperature. The specific endorhamnosidase activities of Sf6 tailspike protein toward fluorescence-labeled dodeca-, deca-, and octasaccharide fragments of Shigella O-antigen suggest a similar active site topology of both proteins. Upon deletion of the N-terminal putative capsid-binding domain, the protein still forms a thermostable, SDS-resistant trimer that has been crystallized. The observations strongly suggest that the tailspike of phage Sf6 is a trimeric parallel -helix protein with high structural similarity to its functional homolog from phage P22. | - |
dc.description.statementofresponsibility | Alexander Freiberg, Renato Morona, Luisa Van Den Bosch, Christiane Jung, Joachim Behlke, Nils Carlin, Robert Seckler, and Ulrich Baxa | - |
dc.language.iso | en | - |
dc.publisher | Amer Soc Biochemistry Molecular Biology Inc | - |
dc.rights | Copyright © 2003 by the American Society for Biochemistry and Molecular Biology. | - |
dc.source.uri | http://www.jbc.org/cgi/content/abstract/278/3/1542 | - |
dc.subject | Shigella | - |
dc.subject | Bacteriophage P22 | - |
dc.subject | Glycoside Hydrolases | - |
dc.subject | Viral Tail Proteins | - |
dc.subject | DNA Primers | - |
dc.subject | Electrophoresis, Polyacrylamide Gel | - |
dc.subject | Spectroscopy, Fourier Transform Infrared | - |
dc.subject | Circular Dichroism | - |
dc.subject | Cloning, Molecular | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Base Sequence | - |
dc.subject | Protein Structure, Secondary | - |
dc.subject | Molecular Sequence Data | - |
dc.title | The tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the β-helix domain | - |
dc.title.alternative | The tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1074/jbc.M205294200 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Morona, R. [0000-0001-7009-7440] | - |
Appears in Collections: | Aurora harvest 6 Molecular and Biomedical Science publications |
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