Structural studies of the Fur protein from Rhizobium leguminosarum

Kolade, O. O., Bellini, P., Wexler, M., Johnston, A. W. B., Grossmann, J. G. and Hemmings, A. M. (2002) Structural studies of the Fur protein from Rhizobium leguminosarum. Biochemical Society Transactions, 30 (4). pp. 771-774. ISSN 1470-8752

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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 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.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Plant Sciences Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017)
Depositing User:	EPrints Services
Date Deposited:	01 Oct 2010 13:36
Last Modified:	06 Feb 2025 03:46
URI:	https://ueaeprints.uea.ac.uk/id/eprint/458
DOI:	10.1042/BST0300771

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