Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase
| Autor: | Catherine L. Drennan, Edward J. Brignole, Elizabeth C. Wittenborn, Samuel Thompson, Mehmet Can, Stephen W. Ragsdale, Steven E. Cohen |
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| Rok vydání: | 2020 |
| Předmět: |
Stereochemistry
Iron Molecular Dynamics Simulation Article 03 medical and health sciences chemistry.chemical_compound Corrinoid Bacterial Proteins Protein Domains Structural Biology Moorella thermoacetica Multienzyme Complexes Nickel Moorella Molecular Biology 030304 developmental biology 0303 health sciences biology ATP synthase 030302 biochemistry & molecular biology Acetyl-CoA Methylation biology.organism_classification Negative stain Aldehyde Oxidoreductases chemistry Acetogenesis biology.protein Sulfur Carbon monoxide dehydrogenase |
| Zdroj: | Structure |
| ISSN: | 1878-4186 |
| Popis: | The nickel-iron-sulfur-containing A-cluster of acetyl-CoA synthase (ACS) assembles acetyl-CoA from carbon monoxide (CO), a methyl group (CH(3)(+)), and coenzyme A (CoA). To accomplish this feat, ACS must bind CoA and interact with two other proteins that contribute the CO and CH(3)(+), respectively: carbon monoxide dehydrogenase (CODH) and corrinoid iron-sulfur protein (CFeSP). Previous structural data show that in the model acetogen Moorella thermoacetica, domain 1 of ACS binds to CODH such that a 70-Å-long internal channel is created that allows for CO to travel from CODH to the A-cluster. The A-cluster is largely buried and is inaccessible to CFeSP for methylation. Here we use electron microscopy to capture multiple snapshots of ACS that reveal previously uncharacterized domain motion, forming extended and hyperextended structural states. In these structural states, the A-cluster is accessible for methylation by CFeSP. |
| Databáze: | OpenAIRE |
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