Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase
Copyright © 2020 American Chemical Society. The Wood-Ljungdahl pathway allows for autotrophic bacterial growth on carbon dioxide, with the last step in acetyl-CoA synthesis catalyzed by the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS). ACS uses a complex Ni-Fe-S m...
| Main Authors: | , , , , , |
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| Other Authors: | |
| Format: | Article |
| Language: | English |
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American Chemical Society (ACS)
2021
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| Online Access: | https://hdl.handle.net/1721.1/133251 |
| _version_ | 1811094470956941312 |
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| author | Cohen, Steven E Can, Mehmet Wittenborn, Elizabeth C Hendrickson, Rachel A Ragsdale, Stephen W Drennan, Catherine L |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Cohen, Steven E Can, Mehmet Wittenborn, Elizabeth C Hendrickson, Rachel A Ragsdale, Stephen W Drennan, Catherine L |
| author_sort | Cohen, Steven E |
| collection | MIT |
| description | Copyright © 2020 American Chemical Society. The Wood-Ljungdahl pathway allows for autotrophic bacterial growth on carbon dioxide, with the last step in acetyl-CoA synthesis catalyzed by the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS). ACS uses a complex Ni-Fe-S metallocluster termed the A-cluster to assemble acetyl-CoA from carbon monoxide, a methyl moiety and coenzyme A. Here, we report the crystal structure of CODH/ACS from Moorella thermoacetica with substrate carbon monoxide bound at the A-cluster, a state previously uncharacterized by crystallography. Direct structural characterization of this state highlights the role of second sphere residues and conformational dynamics in acetyl-CoA assembly, the biological equivalent of the Monsanto process. |
| first_indexed | 2024-09-23T16:00:30Z |
| format | Article |
| id | mit-1721.1/133251 |
| institution | Massachusetts Institute of Technology |
| language | English |
| last_indexed | 2024-09-23T16:00:30Z |
| publishDate | 2021 |
| publisher | American Chemical Society (ACS) |
| record_format | dspace |
| spelling | mit-1721.1/1332512023-01-20T21:49:26Z Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase Cohen, Steven E Can, Mehmet Wittenborn, Elizabeth C Hendrickson, Rachel A Ragsdale, Stephen W Drennan, Catherine L Massachusetts Institute of Technology. Department of Chemistry Massachusetts Institute of Technology. Department of Biology Copyright © 2020 American Chemical Society. The Wood-Ljungdahl pathway allows for autotrophic bacterial growth on carbon dioxide, with the last step in acetyl-CoA synthesis catalyzed by the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS). ACS uses a complex Ni-Fe-S metallocluster termed the A-cluster to assemble acetyl-CoA from carbon monoxide, a methyl moiety and coenzyme A. Here, we report the crystal structure of CODH/ACS from Moorella thermoacetica with substrate carbon monoxide bound at the A-cluster, a state previously uncharacterized by crystallography. Direct structural characterization of this state highlights the role of second sphere residues and conformational dynamics in acetyl-CoA assembly, the biological equivalent of the Monsanto process. 2021-10-27T19:51:47Z 2021-10-27T19:51:47Z 2020 2021-08-13T14:18:05Z Article http://purl.org/eprint/type/JournalArticle https://hdl.handle.net/1721.1/133251 en 10.1021/ACSCATAL.0C03033 ACS Catalysis Creative Commons Attribution-NonCommercial-NoDerivs License http://creativecommons.org/licenses/by-nc-nd/4.0/ application/pdf American Chemical Society (ACS) ACS |
| spellingShingle | Cohen, Steven E Can, Mehmet Wittenborn, Elizabeth C Hendrickson, Rachel A Ragsdale, Stephen W Drennan, Catherine L Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase |
| title | Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase |
| title_full | Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase |
| title_fullStr | Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase |
| title_full_unstemmed | Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase |
| title_short | Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase |
| title_sort | crystallographic characterization of the carbonylated a cluster in carbon monoxide dehydrogenase acetyl coa synthase |
| url | https://hdl.handle.net/1721.1/133251 |
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