5AA5

Actinobacterial-type NiFe-hydrogenase from Ralstonia eutropha H16 at 2.85 Angstrom resolution

5AA5 の概要

• エントリーDOI: 10.2210/pdb5aa5/pdb
• 分子名称: NIFE-HYDROGENASE SMALL SUBUNIT, HOFK, NIFE-HYDROGENASE LARGE SUBUNIT, HOFG, IRON/SULFUR CLUSTER, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, hydrogenase, dihydrogen, metalloenzyme, nickel, tropospheric hydrogen, oxygen tolerance
• 由来する生物種: CUPRIAVIDUS NECATOR (RALSTONIA EUTROPHA); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 628610.33

構造登録者

Schaefer, C.,Bommer, M.,Hennig, S.,Jeoung, J.H.,Dobbek, H.,Lenz, O. (登録日: 2015-07-23, 公開日: 2016-01-20, 最終更新日: 2024-11-20)

主引用文献

Schafer, C.,Bommer, M.,Hennig, S.E.,Jeoung, J.,Dobbek, H.,Lenz, O.
Structure of an Actinobacterial-Type [Nife]-Hydrogenase Reveals Insight Into O2-Tolerant H2 Oxidation.
Structure, 24:285-, 2016

PubMed Abstract: A novel group of bacterial [NiFe]-hydrogenases is responsible for high-affinity H2 uptake from the troposphere, and is therefore thought to play an important role in the global H2 cycle. Here we present the first crystal structure at 2.85-Å resolution of such an actinobacterial-type hydrogenase (AH), which was isolated from the dihydrogen oxidizing bacterium, Ralstonia eutropha. The enzyme has a dimeric structure carrying two active [NiFe] sites that are interconnected by six [4Fe4S] clusters over a range of approximately 90 Å. Unlike most other [NiFe]-hydrogenases, the [4Fe4S] cluster proximal to the [NiFe] site is coordinated by three cysteines and one aspartate. Mutagenesis experiments revealed that this aspartate residue is related to the apparent O2 insensitivity of the AH. Our data provide first structural insight into specialized hydrogenases that are supposed to consume atmospheric H2 under challenging conditions, i.e. at high O2 concentration and wide temperature and pH ranges.

PubMed: 26749450
DOI: 10.1016/J.STR.2015.11.010

実験手法

X-RAY DIFFRACTION (2.497 Å)