Structural studies of the Fur protein from Rhizobium leguminosarum

O. O. Kolade, P. Bellini, M. Wexler, A. W. B. Johnston, J. G. Grossmann, A. M. Hemmings

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)771-774
Number of pages4
JournalBiochemical Society Transactions
Volume30
Issue number4
DOIs
Publication statusPublished - 2002

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