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TitleNegative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase.
Journal, issue, pagesStructure, Vol. 29, Issue 1, Page 43-49.e3, Year 2021
Publish dateJan 7, 2021
AuthorsSteven E Cohen / Edward J Brignole / Elizabeth C Wittenborn / Mehmet Can / Samuel Thompson / Stephen W Ragsdale / Catherine L Drennan /
PubMed AbstractThe Ni-Fe-S-containing A-cluster of acetyl-coenzyme A (CoA) synthase (ACS) assembles acetyl-CoA from carbon monoxide (CO), a methyl group (CH), and CoA. To accomplish this feat, ACS must bind CoA and ...The Ni-Fe-S-containing A-cluster of acetyl-coenzyme A (CoA) synthase (ACS) assembles acetyl-CoA from carbon monoxide (CO), a methyl group (CH), and CoA. To accomplish this feat, ACS must bind CoA and interact with two other proteins that contribute the CO and CH, respectively: CO dehydrogenase (CODH) and corrinoid Fe-S 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 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.
External linksStructure / PubMed:32937101 / PubMed Central
MethodsEM (single particle)
Resolution44.8 - 46.7 Å
Structure data

EMDB-21005:
Negative stain EM map of CODH/ACS in the closed conformation
Method: EM (single particle) / Resolution: 44.8 Å

EMDB-21006:
Negative stain EM map of CODH/ACS in the hyperextended conformation
Method: EM (single particle) / Resolution: 46.7 Å

EMDB-21007:
Negative stain EM map of CODH/ACS in the half-extended conformation
Method: EM (single particle) / Resolution: 46.7 Å

EMDB-21008:
Negative stain EM map of CODH/ACS in the extended conformation
Method: EM (single particle) / Resolution: 45.9 Å

Source
  • Moorella thermoacetica (bacteria)

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