Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase

© 2020 Elsevier Ltd Cohen et al. demonstrate that carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) undergoes wider conformational changes than previously reported. Furthermore, these new conformations explain how the ACS subunit can interact with corrinoid Fe-S protein (CFeSP) in order t...

Full description

Bibliographic Details
Main Authors: Cohen, Steven E, Brignole, Edward J, Wittenborn, Elizabeth C, Can, Mehmet, Thompson, Samuel, Ragsdale, Stephen W, Drennan, Catherine L
Other Authors: Massachusetts Institute of Technology. Department of Chemistry
Format: Article
Language:English
Published: Elsevier BV 2022
Online Access:https://hdl.handle.net/1721.1/139663
_version_ 1826215383721312256
author Cohen, Steven E
Brignole, Edward J
Wittenborn, Elizabeth C
Can, Mehmet
Thompson, Samuel
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
Brignole, Edward J
Wittenborn, Elizabeth C
Can, Mehmet
Thompson, Samuel
Ragsdale, Stephen W
Drennan, Catherine L
author_sort Cohen, Steven E
collection MIT
description © 2020 Elsevier Ltd Cohen et al. demonstrate that carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) undergoes wider conformational changes than previously reported. Furthermore, these new conformations explain how the ACS subunit can interact with corrinoid Fe-S protein (CFeSP) in order to mediate a methyl transfer reaction instrumental for anaerobic carbon fixation.
first_indexed 2024-09-23T16:26:38Z
format Article
id mit-1721.1/139663
institution Massachusetts Institute of Technology
language English
last_indexed 2024-09-23T16:26:38Z
publishDate 2022
publisher Elsevier BV
record_format dspace
spelling mit-1721.1/1396632023-02-14T20:36:46Z Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase Cohen, Steven E Brignole, Edward J Wittenborn, Elizabeth C Can, Mehmet Thompson, Samuel Ragsdale, Stephen W Drennan, Catherine L Massachusetts Institute of Technology. Department of Chemistry Massachusetts Institute of Technology. Department of Biology Howard Hughes Medical Institute © 2020 Elsevier Ltd Cohen et al. demonstrate that carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) undergoes wider conformational changes than previously reported. Furthermore, these new conformations explain how the ACS subunit can interact with corrinoid Fe-S protein (CFeSP) in order to mediate a methyl transfer reaction instrumental for anaerobic carbon fixation. 2022-01-24T15:44:10Z 2022-01-24T15:44:10Z 2021 2022-01-24T15:38:40Z Article http://purl.org/eprint/type/JournalArticle https://hdl.handle.net/1721.1/139663 Cohen, Steven E, Brignole, Edward J, Wittenborn, Elizabeth C, Can, Mehmet, Thompson, Samuel et al. 2021. "Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase." Structure, 29 (1). en 10.1016/J.STR.2020.08.011 Structure Creative Commons Attribution-NonCommercial-NoDerivs License http://creativecommons.org/licenses/by-nc-nd/4.0/ application/pdf Elsevier BV PMC
spellingShingle Cohen, Steven E
Brignole, Edward J
Wittenborn, Elizabeth C
Can, Mehmet
Thompson, Samuel
Ragsdale, Stephen W
Drennan, Catherine L
Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase
title Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase
title_full Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase
title_fullStr Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase
title_full_unstemmed Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase
title_short Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase
title_sort negative stain electron microscopy reveals dramatic structural rearrangements in ni fe s dependent carbon monoxide dehydrogenase acetyl coa synthase
url https://hdl.handle.net/1721.1/139663
work_keys_str_mv AT cohenstevene negativestainelectronmicroscopyrevealsdramaticstructuralrearrangementsinnifesdependentcarbonmonoxidedehydrogenaseacetylcoasynthase
AT brignoleedwardj negativestainelectronmicroscopyrevealsdramaticstructuralrearrangementsinnifesdependentcarbonmonoxidedehydrogenaseacetylcoasynthase
AT wittenbornelizabethc negativestainelectronmicroscopyrevealsdramaticstructuralrearrangementsinnifesdependentcarbonmonoxidedehydrogenaseacetylcoasynthase
AT canmehmet negativestainelectronmicroscopyrevealsdramaticstructuralrearrangementsinnifesdependentcarbonmonoxidedehydrogenaseacetylcoasynthase
AT thompsonsamuel negativestainelectronmicroscopyrevealsdramaticstructuralrearrangementsinnifesdependentcarbonmonoxidedehydrogenaseacetylcoasynthase
AT ragsdalestephenw negativestainelectronmicroscopyrevealsdramaticstructuralrearrangementsinnifesdependentcarbonmonoxidedehydrogenaseacetylcoasynthase
AT drennancatherinel negativestainelectronmicroscopyrevealsdramaticstructuralrearrangementsinnifesdependentcarbonmonoxidedehydrogenaseacetylcoasynthase