Structural studies of the Fur protein from Rhizobium leguminosarum |
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Authors: | Kolade O O Bellini P Wexler M Johnston A W B Grossmann J G Hemmings A M |
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Affiliation: | School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK. |
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Abstract: | The X-ray crystal structure of the apo-form of the Fur protein from Rhizobium leguminosarum has been solved at 2.7 A resolution. Small-angle X-ray scattering was used to give information on the solution conformation of the protein. The Fur homodimer folds into two domains. The N-terminal domain is formed from the packing of two helix-turn-helix motifs while the C-terminal domain appears primarily to stabilize the dimeric state of the protein. |
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