7Z0S

Structure of the Escherichia coli formate hydrogenlyase complex (anaerobic preparation, without formate dehydrogenase H)

7Z0S の概要

• エントリーDOI: 10.2210/pdb7z0s/pdb
• EMDBエントリー: 14429
• 分子名称: Formate hydrogenlyase subunit 3, CARBONMONOXIDE-(DICYANO) IRON, 1-CIS-9-OCTADECANOYL-2-CIS-9-HEXADECANOYL PHOSPHATIDYL GLYCEROL, ... (15 entities in total)
• 機能のキーワード: fhl, group-4 membrane bound hydrogenase, [nife] hydrogenase, membrane protein
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 241425.81

構造登録者

Steinhilper, R.,Murphy, B.J. (登録日: 2022-02-23, 公開日: 2022-09-28, 最終更新日: 2024-07-17)

主引用文献

Steinhilper, R.,Hoff, G.,Heider, J.,Murphy, B.J.
Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli.
Nat Commun, 13:5395-5395, 2022

PubMed Abstract: The prototypical hydrogen-producing enzyme, the membrane-bound formate hydrogenlyase (FHL) complex from Escherichia coli, links formate oxidation at a molybdopterin-containing formate dehydrogenase to proton reduction at a [NiFe] hydrogenase. It is of intense interest due to its ability to efficiently produce H during fermentation, its reversibility, allowing H-dependent CO reduction, and its evolutionary link to respiratory complex I. FHL has been studied for over a century, but its atomic structure remains unknown. Here we report cryo-EM structures of FHL in its aerobically and anaerobically isolated forms at resolutions reaching 2.6 Å. This includes well-resolved density for conserved loops linking the soluble and membrane arms believed to be essential in coupling enzymatic turnover to ion translocation across the membrane in the complex I superfamily. We evaluate possible structural determinants of the bias toward hydrogen production over its oxidation and describe an unpredicted metal-binding site near the interface of FdhF and HycF subunits that may play a role in redox-dependent regulation of FdhF interaction with the complex.

PubMed: 36104349
DOI: 10.1038/s41467-022-32831-x

実験手法

ELECTRON MICROSCOPY (2.6 Å)