3AV8

Refined Structure of Plant-type [2Fe-2S] Ferredoxin I from Aphanothece sacrum at 1.46 A Resolution

3AV8 の概要

• エントリーDOI: 10.2210/pdb3av8/pdb
• 関連するPDBエントリー: 1FXI
• 分子名称: Ferredoxin-1, FE2/S2 (INORGANIC) CLUSTER, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: beta-grasp, redox protein, electron transport
• 由来する生物種: Aphanothece sacrum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 42493.00

構造登録者

Kameda, H.,Hirabayashi, K.,Wada, K.,Fukuyama, K. (登録日: 2011-02-28, 公開日: 2012-01-11, 最終更新日: 2023-11-01)

主引用文献

Kameda, H.,Hirabayashi, K.,Wada, K.,Fukuyama, K.
Mapping of protein-protein interaction sites in the plant-type [2Fe-2S] ferredoxin.
Plos One, 6:e21947-e21947, 2011

PubMed Abstract: Knowing the manner of protein-protein interactions is vital for understanding biological events. The plant-type [2Fe-2S] ferredoxin (Fd), a well-known small iron-sulfur protein with low redox potential, partitions electrons to a variety of Fd-dependent enzymes via specific protein-protein interactions. Here we have refined the crystal structure of a recombinant plant-type Fd I from the blue green alga Aphanothece sacrum (AsFd-I) at 1.46 Å resolution on the basis of the synchrotron radiation data. Incorporating the revised amino-acid sequence, our analysis corrects the 3D structure previously reported; we identified the short α-helix (67-71) near the active center, which is conserved in other plant-type [2Fe-2S] Fds. Although the 3D structures of the four molecules in the asymmetric unit are similar to each other, detailed comparison of the four structures revealed the segments whose conformations are variable. Structural comparison between the Fds from different sources showed that the distribution of the variable segments in AsFd-I is highly conserved in other Fds, suggesting the presence of intrinsically flexible regions in the plant-type [2Fe-2S] Fd. A few structures of the complexes with Fd-dependent enzymes clearly demonstrate that the protein-protein interactions are achieved through these variable regions in Fd. The results described here will provide a guide for interpreting the biochemical and mutational studies that aim at the manner of interactions with Fd-dependent enzymes.

PubMed: 21760931
DOI: 10.1371/journal.pone.0021947

実験手法

X-RAY DIFFRACTION (1.46 Å)