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TitleDeep-branching evolutionary intermediates reveal structural origins of form I rubisco.
Journal, issue, pagesCurr Biol, Vol. 33, Issue 24, Page 5316-55325.e3, Year 2023
Publish dateDec 18, 2023
AuthorsAlbert K Liu / Benjamin Kaeser / LinXing Chen / Jacob West-Roberts / Leah J Taylor-Kearney / Adi Lavy / Damian Günzing / Wen-Jun Li / Michal Hammel / Eva Nogales / Jillian F Banfield / Patrick M Shih /
PubMed AbstractThe enzyme rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) catalyzes the majority of biological carbon fixation on Earth. Although the vast majority of rubiscos across the tree of life ...The enzyme rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) catalyzes the majority of biological carbon fixation on Earth. Although the vast majority of rubiscos across the tree of life assemble as homo-oligomers, the globally predominant form I enzyme-found in plants, algae, and cyanobacteria-forms a unique hetero-oligomeric complex. The recent discovery of a homo-oligomeric sister group to form I rubisco (named form I') has filled a key gap in our understanding of the enigmatic origins of the form I clade. However, to elucidate the series of molecular events leading to the evolution of form I rubisco, we must examine more distantly related sibling clades to contextualize the molecular features distinguishing form I and form I' rubiscos. Here, we present a comparative structural study retracing the evolutionary history of rubisco that reveals a complex structural trajectory leading to the ultimate hetero-oligomerization of the form I clade. We structurally characterize the oligomeric states of deep-branching form Iα and I'' rubiscos recently discovered from metagenomes, which represent key evolutionary intermediates preceding the form I clade. We further solve the structure of form I'' rubisco, revealing the molecular determinants that likely primed the enzyme core for the transition from a homo-oligomer to a hetero-oligomer. Our findings yield new insight into the evolutionary trajectory underpinning the adoption and entrenchment of the prevalent assembly of form I rubisco, providing additional context when viewing the enzyme family through the broader lens of protein evolution.
External linksCurr Biol / PubMed:37979578
MethodsEM (single particle)
Resolution2.21 Å
Structure data

41946

8u66

EMDB-41946, PDB-8u66:
Firmicutes Rubisco
Method: EM (single particle) / Resolution: 2.21 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-CAP:
2-CARBOXYARABINITOL-1,5-DIPHOSPHATE

ChemComp-HOH:
WATER / Water

Source
  • bacillota (low GC Gram+)
KeywordsLYASE / Carboxylase / Oxygenase

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