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Article

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

Cell - 15 Jun 2007

Saschenbrecker Sandra, Bracher Andreas, Rao Karnam Vasudeva, Rao Bharathi Vasudeva, Hartl F Ulrich, Hayer-Hartl Manajit

Abstract excerpt

After folding, many proteins must assemble into oligomeric complexes to become biologically active. Here we describe the role of RbcX as an assembly chaperone of ribulose-bisphosphate carboxylase/oxygenase (Rubisco), the enzyme responsible for the fixation of atmospheric carbon dioxide. In cyanobacteria and plants, Rubisco is an approximately 520 kDa complex composed of eight large subunits (RbcL) and eight small...

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Share to Crystallography, X-Ray
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Structure, Tertiary

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Share to Sequence Homology, Amino Acid

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Source

Identifiers

PMID: 17574029
DOI: 10.1016/j.cell.2007.04.025

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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