6URA

Crystal structure of RUBISCO from Promineofilum breve

Summary for 6URA

• Entry DOI: 10.2210/pdb6ura/pdb
• Descriptor: Ribulose bisphosphate carboxylase large chain, 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: rubisco carboxylase, lyase
• Biological source: Candidatus Promineofilum breve
• Total number of polymer chains: 4
• Total formula weight: 206453.29

Authors

Pereira, J.H.,Banda, D.M.,Liu, A.K.,Shih, P.M.,Adams, P.D. (deposition date: 2019-10-23, release date: 2020-08-19, Last modification date: 2023-11-15)

Primary citation

Banda, D.M.,Pereira, J.H.,Liu, A.K.,Orr, D.J.,Hammel, M.,He, C.,Parry, M.A.J.,Carmo-Silva, E.,Adams, P.D.,Banfield, J.F.,Shih, P.M.
Novel bacterial clade reveals origin of form I Rubisco.
Nat.Plants, 6:1158-1166, 2020

PubMed Abstract: Rubisco sustains the biosphere through the fixation of CO into biomass. In plants and cyanobacteria, form I Rubisco is structurally comprised of large and small subunits, whereas all other Rubisco forms lack small subunits. The rise of the form I complex through the innovation of small subunits represents a key, yet poorly understood, transition in Rubisco's evolution. Through metagenomic analyses, we discovered a previously uncharacterized clade sister to form I Rubisco that evolved without small subunits. This clade diverged before the evolution of cyanobacteria and the origin of the small subunit; thus, it provides a unique reference point to advance our understanding of form I Rubisco evolution. Structural and kinetic data presented here reveal how a proto-form I Rubisco assembled and functioned without the structural stability imparted from small subunits. Our findings provide insight into a key evolutionary transition of the most abundant enzyme on Earth and the predominant entry point for nearly all global organic carbon.

PubMed: 32868887
DOI: 10.1038/s41477-020-00762-4

Experimental method

X-RAY DIFFRACTION (2.17 Å)