6EKB
Crystal structure of the BSD2 homolog of Arabidopsis thaliana
Summary for 6EKB
| Entry DOI | 10.2210/pdb6ekb/pdb |
| Descriptor | DnaJ/Hsp40 cysteine-rich domain superfamily protein, ZINC ION (3 entities in total) |
| Functional Keywords | zinc finger, assembly chaperone, rubisco, chaperone |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 8551.70 |
| 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: 2024-05-08) |
| 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 Cited by 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: 29217567DOI: 10.1126/science.aap9221 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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