Predicted topology of the N-terminal domain of the hydrophilic subunit of the mannose transporter of Escherichia coli |
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Authors: | Zora Markovi-Housley Jochen Balbach Beat Stolz Jean-Claude Gnovsio-Taverne |
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Institution: | Zora Markovi?-Housley, Jochen Balbach, Beat Stolz,Jean-Claude Génovésio-Taverne |
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Abstract: | A folding topology for the homodimeric N-terminal domain (IIA, 2 × 14 kDa) of the hydrophilic subunit (IIABman) of the mannose transporter of E. coli is proposed. The prediction is based on (i) tertiary structure prediction methods, and (ii) functional properties of site-directed mutants in correlation with NMR-derived α/β secondary structure data. The 3D structure profile suggested that the overall fold of IIA is similar to that of the unrelated protein, flavodoxin, which is an open-stranded parallel β-sheet with a strand order of 5 4 3 1 2. The 3D model of IIA, constructed using the known atomic structure of flavodoxin, is consistent with the results from site-directed mutagenesis. Recently NMR results confirmed the open parallel β-sheet with a strand order of 4 3 12 (residues 1-120) of our model whereas β-strand 5 (residues 127–130) was shown to be antiparallel to β-strand 4. The correctly predicted fold includes 90% of the monomeric subunit sequence and contains all functional sites of the IIA domain. |
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Keywords: | Mannose transporter α /β protein Protein topology 3D structure prediction |
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