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Structure paper

TitleStructure of the membrane-bound formate hydrogenlyase complex from Escherichia coli.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 5395, Year 2022
Publish dateSep 14, 2022
AuthorsRalf Steinhilper / Gabriele Höff / Johann Heider / Bonnie J Murphy /
PubMed AbstractThe prototypical hydrogen-producing enzyme, the membrane-bound formate hydrogenlyase (FHL) complex from Escherichia coli, links formate oxidation at a molybdopterin-containing formate dehydrogenase ...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.
External linksNat Commun / PubMed:36104349 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 3.4 Å
Structure data

14429

7z0s

EMDB-14429, PDB-7z0s:
Structure of the Escherichia coli formate hydrogenlyase complex (anaerobic preparation, without formate dehydrogenase H)
Method: EM (single particle) / Resolution: 2.6 Å

14430

7z0t

EMDB-14430, PDB-7z0t:
Structure of the Escherichia coli formate hydrogenlyase complex (aerobic preparation, composite structure)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-14431: Structure of the Escherichia coli formate hydrogenlyase complex (aerobic preparation, consensus refinement)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-14432: Structure of the Escherichia coli formate hydrogenlyase complex (aerobic preparation, focused refinement FdhF)
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-14433: Structure of the Escherichia coli formate hydrogenlyase complex (aerobic preparation, focused refinement peripheral arm)
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-14434: Structure of the Escherichia coli formate hydrogenlyase complex (aerobic preparation, focused refinement membrane arm)
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

ChemComp-NI:
NICKEL (II) ION

ChemComp-FCO:
CARBONMONOXIDE-(DICYANO) IRON

ChemComp-DR9:
1-CIS-9-OCTADECANOYL-2-CIS-9-HEXADECANOYL PHOSPHATIDYL GLYCEROL

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-FE:
Unknown entry

ChemComp-LMN:
Lauryl Maltose Neopentyl Glycol / detergent*YM

ChemComp-HOH:
WATER

ChemComp-MGD:
2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE

ChemComp-6MO:
Unknown entry

Source
  • Escherichia coli (E. coli)
  • escherichia coli k-12 (bacteria)
KeywordsMEMBRANE PROTEIN / FHL / group-4 membrane bound hydrogenase / [NiFe] hydrogenase

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