2Z1F

Crystal structure of HypE from Thermococcus kodakaraensis (inward form)

2Z1F の概要

• エントリーDOI: 10.2210/pdb2z1f/pdb
• 関連するPDBエントリー: 2Z1C 2Z1D 2Z1E
• 分子名称: Hydrogenase expression/formation protein HypE (2 entities in total)
• 機能のキーワード: [nife] hydrogenase maturation, atpase, transferase
• 由来する生物種: Thermococcus kodakarensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35954.43

構造登録者

Watanabe, S.,Matsumi, R.,Arai, T.,Atomi, H.,Imanaka, T.,Miki, K. (登録日: 2007-05-08, 公開日: 2007-07-17, 最終更新日: 2024-03-13)

主引用文献

Watanabe, S.,Matsumi, R.,Arai, T.,Atomi, H.,Imanaka, T.,Miki, K.
Crystal Structures of [NiFe] Hydrogenase Maturation Proteins HypC, HypD, and HypE: Insights into Cyanation Reaction by Thiol Redox Signaling
Mol.Cell, 27:29-40, 2007

PubMed Abstract: [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE catalyze the insertion and cyanation of the iron center of [NiFe] hydrogenases by an unknown mechanism. We have determined the crystal structures of HypC, HypD, and HypE from Thermococcus kodakaraensis KOD1 at 1.8 A, 2.07 A, and 1.55 A resolution, respectively. The structure of HypD reveals its probable iron binding and active sites for cyanation. An extended conformation of each conserved motif of HypC and HypE allows the essential cysteine residues of both proteins to interact with the active site of HypD. Furthermore, the C-terminal tail of HypE is shown to exist in an ATP-dependent dynamic equilibrium between outward and inward conformations. Unexpectedly, the [4Fe-4S] cluster environment of HypD is quite similar to that of ferredoxin:thioredoxin reductase (FTR), indicating the existence of a redox cascade similar to the FTR system. These results suggest a cyanation reaction mechanism via unique thiol redox signaling in the HypCDE complex.

PubMed: 17612488
DOI: 10.1016/j.molcel.2007.05.039

実験手法

X-RAY DIFFRACTION (1.7 Å)