7Z0S
Structure of the Escherichia coli formate hydrogenlyase complex (anaerobic preparation, without formate dehydrogenase H)
Summary for 7Z0S
| Entry DOI | 10.2210/pdb7z0s/pdb |
| EMDB information | 14429 |
| Descriptor | Formate hydrogenlyase subunit 3, CARBONMONOXIDE-(DICYANO) IRON, 1-CIS-9-OCTADECANOYL-2-CIS-9-HEXADECANOYL PHOSPHATIDYL GLYCEROL, ... (15 entities in total) |
| Functional Keywords | fhl, group-4 membrane bound hydrogenase, [nife] hydrogenase, membrane protein |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 6 |
| Total formula weight | 241425.81 |
| Authors | Steinhilper, R.,Murphy, B.J. (deposition date: 2022-02-23, release date: 2022-09-28, Last modification date: 2024-07-17) |
| Primary citation | 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 Cited by 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: 36104349DOI: 10.1038/s41467-022-32831-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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