2W57

Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals structural rearrangement of the DNA-binding domains

2W57 の概要

• エントリーDOI: 10.2210/pdb2w57/pdb
• 分子名称: FERRIC UPTAKE REGULATION PROTEIN, ZINC ION (3 entities in total)
• 機能のキーワード: gene regulation, vibrio cholerae, transcription regulation, metal transport, iron, repressor, dna-binding, transcription, metal-binding, ferric uptake
• 由来する生物種: VIBRIO CHOLERAE
• 細胞内の位置: Cytoplasm (By similarity): P0C6C8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34137.90

構造登録者

Sheikh, M.A.,Taylor, G.L. (登録日: 2008-12-05, 公開日: 2009-01-20, 最終更新日: 2024-11-13)

主引用文献

Sheikh, M.A.,Taylor, G.L.
Crystal Structure of the Vibrio Cholerae Ferric Uptake Regulator (Fur) Reveals Insights Into Metal Co-Ordination.
Mol.Microbiol., 72:1208-, 2009

PubMed Abstract: The ferric uptake regulator (Fur) is a metal-dependent DNA-binding protein that acts as both a repressor and an activator of numerous genes involved in maintaining iron homeostasis in bacteria. It has also been demonstrated in Vibrio cholerae that Fur plays an additional role in pathogenesis, opening up the potential of Fur as a drug target for cholera. Here we present the crystal structure of V. cholerae Fur that reveals a very different orientation of the DNA-binding domains compared with that observed in Pseudomonas aeruginosa Fur. Each monomer of the dimeric Fur protein contains two metal binding sites occupied by zinc in the crystal structure. In the P. aeruginosa study these were designated as the regulatory site (Zn1) and structural site (Zn2). This V. cholerae Fur study, together with studies on Fur homologues and paralogues, suggests that in fact the Zn2 site is the regulatory iron binding site and the Zn1 site plays an auxiliary role. There is no evidence of metal binding to the cysteines that are conserved in many Fur homologues, including Escherichia coli Fur. An analysis of the metal binding properties shows that V. cholerae Fur can be activated by a range of divalent metals.

PubMed: 19400801
DOI: 10.1111/J.1365-2958.2009.06718.X

実験手法

X-RAY DIFFRACTION (2.6 Å)