The X-ray crystal structure of the apo-form of the Fur protein from Rhizobium leguminosarum has been solved at 2.7 å 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.
Structural studies of the Fur protein from Rhizobium leguminosarum
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O. O. Kolade, P. Bellini, M. Wexler, A. W. B. Johnston, J. G. Grossmann, A. M. Hemmings; Structural studies of the Fur protein from Rhizobium leguminosarum. Biochem Soc Trans 1 August 2002; 30 (4): 771–774. doi: https://doi.org/10.1042/bst0300771
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