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TitleCoupled chaperone action in folding and assembly of hexadecameric Rubisco.
Journal, issue, pagesNature, Vol. 463, Issue 7278, Page 197-202, Year 2010
Publish dateJan 14, 2010
AuthorsCuimin Liu / Anna L Young / Amanda Starling-Windhof / Andreas Bracher / Sandra Saschenbrecker / Bharathi Vasudeva Rao / Karnam Vasudeva Rao / Otto Berninghausen / Thorsten Mielke / F Ulrich Hartl / Roland Beckmann / Manajit Hayer-Hartl /
PubMed AbstractForm 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 ...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.
External linksNature / PubMed:20075914
MethodsEM (single particle) / X-ray diffraction
Resolution2.3 - 17.0 Å
Structure data

1654

2wvw

EMDB-1654: Rubisco RbcL8-RbcX2-8 complex
PDB-2wvw: Cryo-EM structure of the RbcL-RbcX complex
Method: EM (single particle) / Resolution: 17.0 Å

1655

2wvw

EMDB-1655: Coupled chaperone action in folding and assembly of hexadecameric Rubisco
PDB-2wvw: Cryo-EM structure of the RbcL-RbcX complex
Method: EM (single particle) / Resolution: 9.0 Å

1656

2wvw

EMDB-1656: Control structure of the RbcL8 octamer
PDB-2wvw: Cryo-EM structure of the RbcL-RbcX complex
Method: EM (single particle) / Resolution: 16.0 Å

PDB-3hyb:
Crystal structure of RbcX from Anabaena, crystal form II
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-HOH:
WATER / Water

Source
  • synechococcus elongatus (bacteria)
  • anabaena sp. (bacteria)
  • anabaena sp. ca (bacteria)
KeywordsPHOTOSYNTHESIS / COMPLEX ASSEMBLY / PHOTORESPIRATION / DISULFIDE BOND / CARBON FIXATION / LYASE / CHAPERONE / CALVIN CYCLE / CARBON DIOXIDE FIXATION / MONOOXYGENASE / METAL-BINDING / OXIDOREDUCTASE / RuBisCO / protein complex assembly

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