Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Membrane-anchored HDCR nanowires drive hydrogen-powered CO fixation.
Journal, issue, pages	Nature, Vol. 607, Issue 7920, Page 823-830, Year 2022
Publish date	Jul 20, 2022
Authors	Helge M Dietrich / Ricardo D Righetto / Anuj Kumar / Wojciech Wietrzynski / Raphael Trischler / Sandra K Schuller / Jonathan Wagner / Fabian M Schwarz / Benjamin D Engel / Volker Müller / Jan M Schuller /
PubMed Abstract	Filamentous enzymes have been found in all domains of life, but the advantage of filamentation is often elusive. Some anaerobic, autotrophic bacteria have an unusual filamentous enzyme for CO ...Filamentous enzymes have been found in all domains of life, but the advantage of filamentation is often elusive. Some anaerobic, autotrophic bacteria have an unusual filamentous enzyme for CO fixation-hydrogen-dependent CO reductase (HDCR)-which directly converts H and CO into formic acid. HDCR reduces CO with a higher activity than any other known biological or chemical catalyst, and it has therefore gained considerable interest in two areas of global relevance: hydrogen storage and combating climate change by capturing atmospheric CO. However, the mechanistic basis of the high catalytic turnover rate of HDCR has remained unknown. Here we use cryo-electron microscopy to reveal the structure of a short HDCR filament from the acetogenic bacterium Thermoanaerobacter kivui. The minimum repeating unit is a hexamer that consists of a formate dehydrogenase (FdhF) and two hydrogenases (HydA2) bound around a central core of hydrogenase Fe-S subunits, one HycB3 and two HycB4. These small bacterial polyferredoxin-like proteins oligomerize through their C-terminal helices to form the backbone of the filament. By combining structure-directed mutagenesis with enzymatic analysis, we show that filamentation and rapid electron transfer through the filament enhance the activity of HDCR. To investigate the structure of HDCR in situ, we imaged T. kivui cells with cryo-electron tomography and found that HDCR filaments bundle into large ring-shaped superstructures attached to the plasma membrane. This supramolecular organization may further enhance the stability and connectivity of HDCR to form a specialized metabolic subcompartment within the cell.
External links	Nature / PubMed:35859174
Methods	EM (single particle) / EM (subtomogram averaging) / EM (tomography)
Resolution	3.4 - 17.0 Å
Structure data	14169 7qv7 EMDB-14169, PDB-7qv7: Cryo-EM structure of Hydrogen-dependent CO2 reductase. Method: EM (single particle) / Resolution: 3.4 Å EMDB-15053: In situ structure of HDCR filaments Method: EM (subtomogram averaging) / Resolution: 17.0 Å EMDB-15054: In situ structure of the T. kivui ribosome Method: EM (subtomogram averaging) / Resolution: 12.0 Å EMDB-15055: In situ cryo-electron tomogram of a T. kivui cell 1 Method: EM (tomography) EMDB-15056: In situ cryo-electron tomogram of a T. kivui cell 2 Method: EM (tomography) EMDB-16451: Subtomogram average of the T. kivui 70S ribosome in situ Method: EM (subtomogram averaging) / Resolution: 7.04 Å
Chemicals	ChemComp-SF4: IRON/SULFUR CLUSTER / Iron–sulfur cluster ChemComp-402: dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS:2kappaS)-mu-(oxomethylidene)diiron(2+)
Source	Thermoanaerobacter kivui LKT-1 (bacteria) thermoanaerobacter kivui (bacteria)
Keywords	ELECTRON TRANSPORT / Hydrogen-dependent CO2 reduction / Carbon fixation / Protein nanowire filament / enzyme catalysis