Structural studies of the Fur protein from Rhizobium leguminosarum. (August 2002)

• Record Type: Journal Article
• Authors: Kolade, O. O.; Bellini, P.; Wexler, M.; Johnston, A. W. B.; Grossmann, J. G.; Hemmings, A. M.
• Is Part Of: Biochemical Society transactions. Volume 30:Number 4(2002)
• Page Start: 771
• Page End: 774
• Publication Date: 2002-08
• Subjects: apo-Fur -- solution X-ray scattering -- X-ray crystallography; Fur, ferric-uptake regulatory protein -- HTH, helix-tum-helix; Biochemistry -- Congresses; 572
• DOI: 10.1042/bst0300771
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : 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.