5CVR

Crystal structure of FNR of A. fischeri in a partially degraded form

5CVR の概要

• エントリーDOI: 10.2210/pdb5cvr/pdb
• 分子名称: FNR type regulator, FE2/S2 (INORGANIC) CLUSTER, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: transcription
• 由来する生物種: Aliivibrio fischeri
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29753.74

構造登録者

Volbeda, A.,Fontecilla-Camps, J.C. (登録日: 2015-07-27, 公開日: 2015-12-16, 最終更新日: 2024-05-01)

主引用文献

Volbeda, A.,Darnault, C.,Renoux, O.,Nicolet, Y.,Fontecilla-Camps, J.C.
The crystal structure of the global anaerobic transcriptional regulator FNR explains its extremely fine-tuned monomer-dimer equilibrium.
Sci Adv, 1:e1501086-e1501086, 2015

PubMed Abstract: The structure of the dimeric holo-fumarate and nitrate reduction regulator (FNR) from Aliivibrio fischeri has been solved at 2.65 Å resolution. FNR globally controls the transition between anaerobic and aerobic respiration in facultative anaerobes through the assembly/degradation of its oxygen-sensitive [4Fe-4S] cluster. In the absence of O2, FNR forms a dimer and specifically binds to DNA, whereas in its presence, the cluster is degraded causing FNR monomerization and DNA dissociation. We have used our crystal structure and the information previously gathered from numerous FNR variants to propose that this process is governed by extremely fine-tuned interactions, mediated by two salt bridges near the amino-terminal cluster-binding domain and an "imperfect" coiled-coil dimer interface. [4Fe-4S] to [2Fe-2S] cluster degradation propagates a conformational signal that indirectly causes monomerization by disrupting the first of these interactions and unleashing the "unzipping" of the FNR dimer in the direction of the carboxyl-terminal DNA binding domain.

PubMed: 26665177
DOI: 10.1126/sciadv.1501086

実験手法

X-RAY DIFFRACTION (2.6 Å)