2WVW

Cryo-EM structure of the RbcL-RbcX complex

Summary for 2WVW

• Entry DOI: 10.2210/pdb2wvw/pdb
• Related: 1RBL 1RSC
• EMDB information: 1655
• Descriptor: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN, RBCX PROTEIN (2 entities in total)
• Functional Keywords: complex assembly, photorespiration, photosynthesis, disulfide bond, carbon fixation, lyase, chaperone, calvin cycle, carbon dioxide fixation, monooxygenase, metal-binding, oxidoreductase
• Biological source: SYNECHOCOCCUS ELONGATUS; More
• Total number of polymer chains: 24
• Total formula weight: 703251.72

Authors

Liu, C.,Young, A.L.,Starling-Windhof, A.,Bracher, A.,Saschenbrecker, S.,Rao, B.V.,Rao, K.V.,Berninghausen, O.,Mielke, T.,Hartl, F.U.,Beckmann, R.,Hayer-Hartl, M. (deposition date: 2009-10-20, release date: 2010-01-19, Last modification date: 2024-11-13)

Primary citation

Liu, C.,Young, A.L.,Starling-Windhof, A.,Bracher, A.,Saschenbrecker, S.,Rao, B.V.,Rao, K.V.,Berninghausen, O.,Mielke, T.,Hartl, F.U.,Beckmann, R.,Hayer-Hartl, M.
Coupled Chaperone Action in Folding and Assembly of Hexadecameric Rubisco
Nature, 463:197-, 2010

PubMed Abstract: Form I Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase), a complex of eight large (RbcL) and eight small (RbcS) subunits, catalyses the fixation of atmospheric CO(2) in photosynthesis. The limited catalytic efficiency of Rubisco has sparked extensive efforts to re-engineer the enzyme with the goal of enhancing agricultural productivity. To facilitate such efforts we analysed the formation of cyanobacterial form I Rubisco by in vitro reconstitution and cryo-electron microscopy. We show that RbcL subunit folding by the GroEL/GroES chaperonin is tightly coupled with assembly mediated by the chaperone RbcX(2). RbcL monomers remain partially unstable and retain high affinity for GroEL until captured by RbcX(2). As revealed by the structure of a RbcL(8)-(RbcX(2))(8) assembly intermediate, RbcX(2) acts as a molecular staple in stabilizing the RbcL subunits as dimers and facilitates RbcL(8) core assembly. Finally, addition of RbcS results in RbcX(2) release and holoenzyme formation. Specific assembly chaperones may be required more generally in the formation of complex oligomeric structures when folding is closely coupled to assembly.

PubMed: 20075914
DOI: 10.1038/NATURE08651

Experimental method

ELECTRON MICROSCOPY (9 Å)