Coupled chaperone action in folding and assembly of hexadecameric Rubisco (Q27658961)

11

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Manajit Hayer-Hartl

object named as

Manajit Hayer-Hartl

12

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Franz-Ulrich Hartl

10

object named as

F Ulrich Hartl

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Amanda Starling-Windhof

3

object named as

Amanda Starling-Windhof

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author name string

Cuimin Liu

1

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Anna L Young

2

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Andreas Bracher

4

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Sandra Saschenbrecker

5

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Bharathi Vasudeva Rao

6

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Karnam Vasudeva Rao

7

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Thorsten Mielke

EMAN: semiautomated software for high-resolution single-particle reconstructions

9

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language of work or name

English

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publication date

14 January 2010

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published in

Nature

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volume

463

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issue

7278

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page(s)

197-202

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cites work

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Assembly of cyanobacterial and higher plant ribulose bisphosphate carboxylase subunits into functional homologous and heterologous enzyme molecules in Escherichia coli

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Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

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Complementing substitutions within loop regions 2 and 3 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase

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Rapid measurement of binding constants and heats of binding using a new titration calorimeter

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The rbcX gene product promotes the production and assembly of ribulose-1,5-bisphosphate carboxylase/oxygenase of Synechococcus sp. PCC7002 in Escherichia coli.

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Structure of the RuBisCO chaperone RbcX from Synechocystis sp. PCC6803

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Rubisco: structure, regulatory interactions, and possibilities for a better enzyme

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Rubisco Synthesis, Assembly, Mechanism, and Regulation

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Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco

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

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The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution.

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Identification of nascent chain interaction sites on trigger factor

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Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7 A resolution

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Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity

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Catalysis and regulation in Rubisco

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UCSF Chimera--a visualization system for exploratory research and analysis

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Structural framework for catalysis and regulation in ribulose-1,5-bisphosphate carboxylase/oxygenase

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Efficient incorporation of unnatural amino acids into proteins in Escherichia coli.

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Catalysis by cyanobacterial ribulose-bisphosphate carboxylase large subunits in the complete absence of small subunits

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Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

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Automated protein model building combined with iterative structure refinement

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Manipulating ribulose bisphosphate carboxylase/oxygenase in the chloroplasts of higher plants

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Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco

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GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

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In vivo photocrosslinking with unnatural amino Acid mutagenesis

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Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

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Heterologous expression and initial characterization of recombinant RbcX protein from Thermosynechococcus elongatus BP-1 and the role of RbcX in RuBisCO assembly.

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Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein.

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Addition of a photocrosslinking amino acid to the genetic code of Escherichiacoli

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Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps

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Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60.

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Function, Structure, and Evolution of the RubisCO-Like Proteins and Their RubisCO Homologs

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Maximum activity of recombinant ribulose 1,5-bisphosphate carboxylase/oxygenase of Anabaena sp. strain CA requires the product of the rbcX gene

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RbcX can function as a rubisco chaperonin, but is non-essential in Synechococcus PCC7942.

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Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding

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Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bishopshate carboxylase in isolated intact pea chloroplasts

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Crossref

https://api.crossref.org/works/10.1038%2FNATURE08651

7 January 2021