7QVI

Fiber-forming RubisCO derived from ancestral sequence reconstruction and rational engineering

Summary for 7QVI

• Entry DOI: 10.2210/pdb7qvi/pdb
• Related: 7QSV 7QSW 7QSX 7QSY 7QSZ 7QT1
• EMDB information: 14178
• Descriptor: RubisCO large subunit, 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• Functional Keywords: ribulose 1, 5-bisphosphate carboxylase/oxydase, rubisco, lyase
• Biological source: synthetic construct
• Total number of polymer chains: 16
• Total formula weight: 825237.60

Authors

Schulz, L.,Zarzycki, J.,Prinz, S.,Schuller, J.M.,Erb, T.J.,Hochberg, G.K.A. (deposition date: 2022-01-21, release date: 2022-10-12, Last modification date: 2022-10-26)

Primary citation

Schulz, L.,Guo, Z.,Zarzycki, J.,Steinchen, W.,Schuller, J.M.,Heimerl, T.,Prinz, S.,Mueller-Cajar, O.,Erb, T.J.,Hochberg, G.K.A.
Evolution of increased complexity and specificity at the dawn of form I Rubiscos.
Science, 378:155-160, 2022

PubMed Abstract: The evolution of ribulose-1,5-bisphosphate carboxylase/oxygenases (Rubiscos) that discriminate strongly between their substrate carbon dioxide and the undesired side substrate dioxygen was an important event for photosynthetic organisms adapting to an oxygenated environment. We use ancestral sequence reconstruction to recapitulate this event. We show that Rubisco increased its specificity and carboxylation efficiency through the gain of an accessory subunit before atmospheric oxygen was present. Using structural and biochemical approaches, we retrace how this subunit was gained and became essential. Our work illuminates the emergence of an adaptation to rising ambient oxygen levels, provides a template for investigating the function of interactions that have remained elusive because of their essentiality, and sheds light on the determinants of specificity in Rubisco.

PubMed: 36227987
DOI: 10.1126/science.abq1416

Experimental method

ELECTRON MICROSCOPY (3 Å)