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Structure determination and refinement of ribulose 1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301.

Newman J, Branden CI, Jones TA
Acta Crystallogr D Biol Crystallogr 49 548-60 (1993)
Cited: 38 times
EuropePMC logo PMID: 15299492

Abstract

The structure of an activated quaternary complex of ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) from Synechococcus PCC6301 has been solved by molecular replacement. The protein crystallizes in an orthorhombic P2(1)2(1)2(1) unit cell with a complete L(8)S(8) complex consisting of 4608 residues (37 680 non-hydrogen atoms) in the asymmetric unit. Data were collected both on film and image plate using synchrotron radiation; there were 218 276 unique reflections in the final 2.2 A data set. The eightfold non-crystallographic symmetry could be used both to improve map quality and to reduce the computing requirements of refinement. The coordinates were refined using strict non-crystallographic symmetry constraints. The stereochemistry of the final model is good, and the model has an R value of 20.0% for the reflections between 7 and 2.2 A.

Reviews - 1rbl mentioned but not cited (2)

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Articles - 1rbl mentioned but not cited (17)

  1. Biochemical characterization of predicted Precambrian RuBisCO. Shih PM, Occhialini A, Cameron JC, Andralojc PJ, Parry MA, Kerfeld CA. Nat Commun 7 10382 (2016)
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  8. Scaffolding protein CcmM directs multiprotein phase separation in β-carboxysome biogenesis. Zang K, Wang H, Hartl FU, Hayer-Hartl M. Nat Struct Mol Biol 28 909-922 (2021)
  9. Structure of Rubisco from Arabidopsis thaliana in complex with 2-carboxyarabinitol-1,5-bisphosphate. Valegård K, Hasse D, Andersson I, Gunn LH. Acta Crystallogr D Struct Biol 74 1-9 (2018)
  10. Constraining the timing of the Great Oxidation Event within the Rubisco phylogenetic tree. Kacar B, Hanson-Smith V, Adam ZR, Boekelheide N. Geobiology 15 628-640 (2017)
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  13. Binding Options for the Small Subunit-Like Domain of Cyanobacteria to Rubisco. Rohnke BA, Kerfeld CA, Montgomery BL. Front Microbiol 11 187 (2020)
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  16. Selection of Cyanobacterial (Synechococcus sp. Strain PCC 6301) RubisCO Variants with Improved Functional Properties That Confer Enhanced CO2-Dependent Growth of Rhodobacter capsulatus, a Photosynthetic Bacterium. Satagopan S, Huening KA, Tabita FR. MBio 10 (2019)
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Reviews citing this publication (6)

  1. Structure and function of Rubisco. Andersson I, Backlund A. Plant Physiol. Biochem. 46 275-291 (2008)
  2. Multiple Rubisco forms in proteobacteria: their functional significance in relation to CO2 acquisition by the CBB cycle. Badger MR, Bek EJ. J. Exp. Bot. 59 1525-1541 (2008)
  3. Phylogenetic and evolutionary relationships of RubisCO and the RubisCO-like proteins and the functional lessons provided by diverse molecular forms. Tabita FR, Hanson TE, Satagopan S, Witte BH, Kreel NE. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 363 2629-2640 (2008)
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  6. Potential and Challenges of Improving Photosynthesis in Algae. Vecchi V, Barera S, Bassi R, Dall'Osto L. Plants (Basel) 9 (2020)

Articles citing this publication (13)

  1. Elucidating essential role of conserved carboxysomal protein CcmN reveals common feature of bacterial microcompartment assembly. Kinney JN, Salmeen A, Cai F, Kerfeld CA. J. Biol. Chem. 287 17729-17736 (2012)
  2. Crystal structure of a novel-type archaeal rubisco with pentagonal symmetry. Kitano K, Maeda N, Fukui T, Atomi H, Imanaka T, Miki K. Structure 9 473-481 (2001)
  3. Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco. Bracher A, Starling-Windhof A, Hartl FU, Hayer-Hartl M. Nat. Struct. Mol. Biol. 18 875-880 (2011)
  4. Opposing effects of folding and assembly chaperones on evolvability of Rubisco. Durão P, Aigner H, Nagy P, Mueller-Cajar O, Hartl FU, Hayer-Hartl M. Nat. Chem. Biol. 11 148-155 (2015)
  5. Structure and mechanism of the Rubisco-assembly chaperone Raf1. Hauser T, Bhat JY, Miličić G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M. Nat. Struct. Mol. Biol. 22 720-728 (2015)
  6. A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration. Satagopan S, Scott SS, Smith TG, Tabita FR. Biochemistry 48 9076-9083 (2009)
  7. Structure of an effector-induced inactivated state of ribulose 1,5-bisphosphate carboxylase/oxygenase: the binary complex between enzyme and xylulose 1,5-bisphosphate. Newman J, Gutteridge S. Structure 2 495-502 (1994)
  8. Mutations in the small subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase increase the formation of the misfire product xylulose-1,5-bisphosphate. Flachmann R, Zhu G, Jensen RG, Bohnert HJ. Plant Physiol. 114 131-136 (1997)
  9. Calcium supports loop closure but not catalysis in Rubisco. Karkehabadi S, Taylor TC, Andersson I. J. Mol. Biol. 334 65-73 (2003)
  10. Molecular basis for the assembly of RuBisCO assisted by the chaperone Raf1. Xia LY, Jiang YL, Kong WW, Sun H, Li WF, Chen Y, Zhou CZ. Nat Plants 6 708-717 (2020)
  11. Complex structure reveals CcmM and CcmN form a heterotrimeric adaptor in β-carboxysome. Sun H, Cui N, Han SJ, Chen ZP, Xia LY, Chen Y, Jiang YL, Zhou CZ. Protein Sci 30 1566-1576 (2021)
  12. Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcX. Li Q, Jiang YL, Xia LY, Chen Y, Zhou CZ. Cell Discov 8 93 (2022)
  13. Novel bacterial clade reveals origin of form I Rubisco. Banda DM, Pereira JH, Liu AK, Orr DJ, Hammel M, He C, Parry MAJ, Carmo-Silva E, Adams PD, Banfield JF, Shih PM. Nat Plants 6 1158-1166 (2020)


Related citations provided by authors (1)

  1. The X-Ray Structure of Synechococcus Ribulose Bisphosphate Carboxylase(Slash)Oxygenase Activated Quaternary Complex at 2.2 Angstroms Resolution. Newman J, Gutteridge S To be published -

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