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TitleStructure and mechanism of the Rubisco-assembly chaperone Raf1.
Journal, issue, pagesNat Struct Mol Biol, Vol. 22, Issue 9, Page 720-728, Year 2015
Publish dateAug 3, 2015
AuthorsThomas Hauser / Javaid Y Bhat / Goran Miličić / Petra Wendler / F Ulrich Hartl / Andreas Bracher / Manajit Hayer-Hartl /
PubMed AbstractBiogenesis of the photosynthetic enzyme Rubisco, a complex of eight large (RbcL) and eight small (RbcS) subunits, requires assembly chaperones. Here we analyzed the role of Rubisco accumulation ...Biogenesis of the photosynthetic enzyme Rubisco, a complex of eight large (RbcL) and eight small (RbcS) subunits, requires assembly chaperones. Here we analyzed the role of Rubisco accumulation factor1 (Raf1), a dimer of ∼40-kDa subunits. We find that Raf1 from Synechococcus elongatus acts downstream of chaperonin-assisted RbcL folding by stabilizing RbcL antiparallel dimers for assembly into RbcL8 complexes with four Raf1 dimers bound. Raf1 displacement by RbcS results in holoenzyme formation. Crystal structures show that Raf1 from Arabidopsis thaliana consists of a β-sheet dimerization domain and a flexibly linked α-helical domain. Chemical cross-linking and EM reconstruction indicate that the β-domains bind along the equator of each RbcL2 unit, and the α-helical domains embrace the top and bottom edges of RbcL2. Raf1 fulfills a role similar to that of the assembly chaperone RbcX, thus suggesting that functionally redundant factors ensure efficient Rubisco biogenesis.
External linksNat Struct Mol Biol / PubMed:26237510
MethodsEM (single particle) / X-ray diffraction
Resolution1.954 - 24.8 Å
Structure data

EMDB-3051:
Structure and mechanism of the Rubisco assembly chaperone Raf1
Method: EM (single particle) / Resolution: 24.8 Å

EMDB-3052:
Structure and mechanism of the Rubisco assembly chaperone Raf1
Method: EM (single particle) / Resolution: 21.4 Å

EMDB-3053:
Structure and mechanism of the Rubisco assembly chaperone Raf1
Method: EM (single particle) / Resolution: 24.6 Å

PDB-4wt3:
The N-terminal domain of Rubisco Accumulation Factor 1 from Arabidopsis thaliana
Method: X-RAY DIFFRACTION / Resolution: 1.954 Å

PDB-4wt4:
The C-terminal domain of Rubisco Accumulation Factor 1 from Arabidopsis thaliana, crystal form I
Method: X-RAY DIFFRACTION / Resolution: 2.81 Å

PDB-4wt5:
The C-terminal domain of Rubisco Accumulation Factor 1 from Arabidopsis thaliana, crystal form II
Method: X-RAY DIFFRACTION / Resolution: 2.568 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • Thermosynechococcus elongatus BP-1 (bacteria)
  • Synechococcus elongatus PCC 6301 (bacteria)
  • arabidopsis thaliana (thale cress)
KeywordsCHAPERONE / assembly chaperone

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