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

Full text not available from this repository. (Request a copy)

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:	24 Sep 2024 10:17
URI:	https://ueaeprints.uea.ac.uk/id/eprint/458
DOI:	10.1042/BST0300771

Actions (login required)

View Item