Part:BBa_M50037
Glucose Binding Protein of Thermus thermophilus
This bacterial glucose binding protein (GBP) is derived from the genome sequence of Thermus thermophilus that was published in 2004 by Henne et al. In 2006, Cuneo et al. analyzed the sequence of this particular GBP, determined its X-ray crystal structure and characterized the stability of glucose-binding. The GBP is composed of two domains separated by a hinge, maintaining an open conformation when unbound to glucose and a closed conformation when bound. When flanked with an RFP fluorophore on the N-terminus and a GFP fluorophore on the C-terminus, these conformation changes facilitated FRET-based analysis of glucose binding. In addition, this GBP was selected for its reasonably short sequence length (1242bp) and stable glucose binding ability (Kd value of 0.08(+/- 0.03) mM). According to Cuneo et al., this T. thermophilus GBP shares more structural homology with maltose binding proteins than glucose binding proteins. However, we were able to obtain FRET when glucose was added, suggesting that glucose is a ligand for this protein.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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