3DAG

The crystal structure of [Fe]-hydrogenase holoenzyme (HMD) from METHANOCALDOCOCCUS JANNASCHII

3DAG の概要

• エントリーDOI: 10.2210/pdb3dag/pdb
• 関連するPDBエントリー: 2BOJ 3DAF 3F46 3F47
• 分子名称: 5,10-methenyltetrahydromethanopterin hydrogenase, FE (II) ION, 5'-O-[(S)-{[2-(carboxymethyl)-6-hydroxy-3,5-dimethylpyridin-4-yl]oxy}(hydroxy)phosphoryl]guanosine, ... (5 entities in total)
• 機能のキーワード: rossmann fold, helix bundle, methanogenesis, one-carbon metabolism, oxidoreductase
• 由来する生物種: Methanocaldococcus jannaschii (Methanococcus jannaschii)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39363.27

構造登録者

Pilak, O.,Warkentin, E.,Shima, S.,Thauer, R.K.,Ermler, U. (登録日: 2008-05-29, 公開日: 2008-12-09, 最終更新日: 2023-08-30)

主引用文献

Shima, S.,Pilak, O.,Vogt, S.,Schick, M.,Stagni, M.S.,Meyer-Klaucke, W.,Warkentin, E.,Thauer, R.K.,Ermler, U.
The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site.
Science, 321:572-575, 2008

PubMed Abstract: Biological formation and consumption of molecular hydrogen (H2) are catalyzed by hydrogenases, of which three phylogenetically unrelated types are known: [NiFe]-hydrogenases, [FeFe]-hydrogenases, and [Fe]-hydrogenase. We present a crystal structure of [Fe]-hydrogenase at 1.75 angstrom resolution, showing a mononuclear iron coordinated by the sulfur of cysteine 176, two carbon monoxide (CO) molecules, and the sp2-hybridized nitrogen of a 2-pyridinol compound with back-bonding properties similar to those of cyanide. The three-dimensional arrangement of the ligands is similar to that of thiolate, CO, and cyanide ligated to the low-spin iron in binuclear [NiFe]- and [FeFe]-hydrogenases, although the enzymes have evolved independently and the CO and cyanide ligands are not found in any other metalloenzyme. The related iron ligation pattern of hydrogenases exemplifies convergent evolution and presumably plays an essential role in H2 activation. This finding may stimulate the ongoing synthesis of catalysts that could substitute for platinum in applications such as fuel cells.

PubMed: 18653896
DOI: 10.1126/science.1158978

実験手法

X-RAY DIFFRACTION (1.75 Å)