Structural studies of the Fur protein from Rhizobium leguminosarum.
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.
School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.
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Kolade
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Bellini
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Wexler
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Johnston
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Grossmann
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Hemmings
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D007501:Iron / Q000378:metabolism*; D008667:Metalloproteins / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D012097:Repressor Proteins / Q000737:chemistry*; D016961:Rhizobium leguminosarum / Q000378:metabolism*
D001426:Bacterial Proteins; D008667:Metalloproteins; D012097:Repressor Proteins; C068477:ferric uptake regulating proteins, bacterial; D007501:Iron