6EKC

Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus

This is a non-PDB format compatible entry.

Summary for 6EKC

• Entry DOI: 10.2210/pdb6ekc/pdb
• Descriptor: Ribulose bisphosphate carboxylase large chain, DnaJ/Hsp40 cysteine-rich domain superfamily protein, ZINC ION, ... (4 entities in total)
• Functional Keywords: zinc finger, assembly chaperone, assembly intermediate, chaperone
• Biological source: Thermosynechococcus elongatus (strain BP-1); More
• Total number of polymer chains: 160
• Total formula weight: 4921404.72

Authors

Aigner, H.,Wilson, R.H.,Bracher, A.,Calisse, L.,Bhat, J.Y.,Hartl, F.U.,Hayer-Hartl, M. (deposition date: 2017-09-26, release date: 2017-12-06, Last modification date: 2024-10-16)

Primary citation

Aigner, H.,Wilson, R.H.,Bracher, A.,Calisse, L.,Bhat, J.Y.,Hartl, F.U.,Hayer-Hartl, M.
Plant RuBisCo assembly in E. coli with five chloroplast chaperones including BSD2.
Science, 358:1272-1278, 2017

PubMed Abstract: Plant RuBisCo, a complex of eight large and eight small subunits, catalyzes the fixation of CO in photosynthesis. The low catalytic efficiency of RuBisCo provides strong motivation to reengineer the enzyme with the goal of increasing crop yields. However, genetic manipulation has been hampered by the failure to express plant RuBisCo in a bacterial host. We achieved the functional expression of RuBisCo in by coexpressing multiple chloroplast chaperones. These include the chaperonins Cpn60/Cpn20, RuBisCo accumulation factors 1 and 2, RbcX, and bundle-sheath defective-2 (BSD2). Our structural and functional analysis revealed the role of BSD2 in stabilizing an end-state assembly intermediate of eight RuBisCo large subunits until the small subunits become available. The ability to produce plant RuBisCo recombinantly will facilitate efforts to improve the enzyme through mutagenesis.

PubMed: 29217567
DOI: 10.1126/science.aap9221

Experimental method

X-RAY DIFFRACTION (2.63 Å)