Structural studies of the Fur protein from Rhizobium leguminosarum

Autor:	Margaret Wexler, Olatomirin O. Kolade, Andrew M. Hemmings, P. Bellini, Andrew W. B. Johnston, J. G. Grossmann
Rok vydání:	2002
Předmět:	Models Molecular Rhizobium leguminosarum Binding Sites Protein Conformation Iron Crystal structure Biology medicine.disease_cause Crystallography X-Ray Biochemistry Repressor Proteins Crystallography Bacterial Proteins Metalloproteins medicine bacteria Amino Acid Sequence Escherichia coli
Zdroj:	Biochemical Society transactions. 30(4)
ISSN:	0300-5127
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07d9aebf9dda9817a99511352ce3766c https://pubmed.ncbi.nlm.nih.gov/12196192 Zobrazit plný text záznamu