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

doi:10.1042/BST0300771

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 journal › Article › peer-review

9 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 language	English
Pages (from-to)	771-774
Number of pages	4
Journal	Biochemical Society Transactions
Volume	30
Issue number	4
DOIs	https://doi.org/10.1042/BST0300771
Publication status	Published - 2002

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10.1042/BST0300771

Cite this

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title = "Structural studies of the Fur protein from Rhizobium leguminosarum",

abstract = "The X-ray crystal structure of the apo-form of the Fur protein from Rhizobium leguminosarum has been solved at 2.7 {\aa} 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.",

author = "Kolade, {O. O.} and P. Bellini and M. Wexler and Johnston, {A. W. B.} and Grossmann, {J. G.} and Hemmings, {A. M.}",

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journal = "Biochemical Society Transactions",

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T1 - Structural studies of the Fur protein from Rhizobium leguminosarum

AU - Kolade, O. O.

AU - Bellini, P.

AU - Wexler, M.

AU - Johnston, A. W. B.

AU - Grossmann, J. G.

AU - Hemmings, A. M.

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

U2 - 10.1042/BST0300771

DO - 10.1042/BST0300771

M3 - Article

SN - 1470-8752

VL - 30

SP - 771

EP - 774

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

IS - 4

ER -