Hypothetical protein Conclusion: Difference between revisions
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A combination of evolutionary, structural and functional have identified hypothetical putative sugar binding protein 2ob5 to belong to the RbsD/FucU superfamily of proteins. Furthermore, through identification and comparison of active sites, key binding residues and conserved regions, it is suggested that 2ob5 is a fucose-binding protein of the FuCU family. It was found that the biological unit of 2ob5's close structural analogs - and potentially 2ob5 - is a decameric non-membrane-bound oligomer. Functional analyses suggest that 2ob5 may catalyse the anomeric change of alpha-purine-fucose to beta-purine-fucose. Limitations in the scope of literature available necessitated some assumptions, and these conclusions would benefit from confirmatory laboratory studies. | |||
[[Hypothetical protein Abstract | Abstract ]] | [[Hypothetical protein Introduction | Introduction]] | [[Hypothetical protein Method| Method]] | | [[Hypothetical protein Abstract | Abstract ]] | [[Hypothetical protein Introduction | Introduction]] | [[Hypothetical protein Method| Method]] | |
Latest revision as of 01:22, 16 June 2009
A combination of evolutionary, structural and functional have identified hypothetical putative sugar binding protein 2ob5 to belong to the RbsD/FucU superfamily of proteins. Furthermore, through identification and comparison of active sites, key binding residues and conserved regions, it is suggested that 2ob5 is a fucose-binding protein of the FuCU family. It was found that the biological unit of 2ob5's close structural analogs - and potentially 2ob5 - is a decameric non-membrane-bound oligomer. Functional analyses suggest that 2ob5 may catalyse the anomeric change of alpha-purine-fucose to beta-purine-fucose. Limitations in the scope of literature available necessitated some assumptions, and these conclusions would benefit from confirmatory laboratory studies.
Abstract | Introduction | Method |
Results | Discussion | Conclusion | References