2GHJ

Crystal structure of folded and partially unfolded forms of Aquifex aeolicus ribosomal protein L20

Summary for 2GHJ

• Entry DOI: 10.2210/pdb2ghj/pdb
• Descriptor: 50S ribosomal protein L20, SULFATE ION (3 entities in total)
• Functional Keywords: folding intermediate; ribosomal protein extension, structural protein
• Biological source: Aquifex aeolicus
• Total number of polymer chains: 4
• Total formula weight: 57289.71

Authors

Timsit, Y.,Allemand, F.,Chiaruttini, C.,Springer, M. (deposition date: 2006-03-27, release date: 2006-04-18, Last modification date: 2024-10-30)

Primary citation

Timsit, Y.,Allemand, F.,Chiaruttini, C.,Springer, M.
Coexistence of two protein folding states in the crystal structure of ribosomal protein L20
Embo Rep., 7:1013-1018, 2006

PubMed Abstract: The recent finding of intrinsically unstructured proteins defies the classical structure-function paradigm. However, owing to their flexibility, intrinsically unstructured proteins generally escape detailed structural investigations. Consequently little is known about the extent of conformational disorder and its role in biological functions. Here, we present the X-ray structure of the unbound ribosomal protein L20, the long basic amino-terminal extension of which has been previously interpreted as fully disordered in the absence of RNA. This study provides the first detailed picture of two protein folding states trapped together in a crystal and indicates that unfolding occurs in discrete regions of the whole protein, corresponding mainly to RNA-binding residues. The electrostatic destabilization of the long alpha-helix and a structural communication between the two L20 domains are reminiscent of those observed in calmodulin. The detailed comparison of the two conformations observed in the crystal provides new insights into the role of unfolded extensions in ribosomal assembly.

PubMed: 16977336
DOI: 10.1038/sj.embor.7400803

Experimental method

X-RAY DIFFRACTION (2.9 Å)