Construction and Characterization of Chimeric Proteins Composed of Type-1 and Type-2 Periplasmic Binding Proteins MglB and ArgT
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概要
- 論文の詳細を見る
The respective type-1 and type-2 periplasmic binding proteins (PBPs) MglB and ArgT are believed to have evolved from a common ancestor into siblings showing topological differences in their main chain connectivity. At first glance, they show similar structure. But, more detailed examination reveals that the chain connectivity of ArgT is more convoluted than that of MglB. Reflecting that complexity, the folding of ArgT is complicated and involves intermediate folds. On the other hand, the folding of MglB is a simple two-state transition. In the present study, we constructed and characterized several chimeras made up of various subdomains of MglB and ArgT with the aim of gaining insight into the evolution of protein folding and protein structure. Although these chimeras did not fold as compactly as their parental proteins, some did exhibit cooperative folding, which suggests that novel proteins with new connectivity and new folding pathways could have emerged at a fairly high rate throughout the evolution of proteins.
- 社団法人 日本農芸化学会の論文
- 2004-04-23
著者
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SHIBA Kiyotaka
Department of Protein Engineering Cancer Institute, Japanese Foundation for Cancer Research
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Nishikawa Ken
Laboratory For Gene-product Informatics National Institute Of Genetics
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Shiba Kiyotaka
Department Of Protein Engineering Cancer Institute Japanese Foundation For Cancer Research
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KASHIWAGI Kenji
Department of Ophthalmology, Yamanashi Medical University
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Fukami (kobayashi)
Bioresource Information Division Riken Bioresource Center
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Kashiwagi K
Department Of Protein Engineering Cancer Institute Japanese Foundation For Cancer Research
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Kashiwagi Kenji
Department Of Ophtalmology Yamanashi Medical University
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Fukami-Kobayashi Kaoru
Bioresource Information Division, RIKEN BioResource Center
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Shiba Kiyotaka
Department of Protein Engineering, Cancer Institute, Japanese Foundation for Cancer Research
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