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. ORCID: https://orcid.org/0000-0003-3053-3134 (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: 21 Jul 2024 00:15
URI: https://ueaeprints.uea.ac.uk/id/eprint/458
DOI: 10.1042/BST0300771

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