6ewn

HspA from Thermosynechococcus vulcanus in the presence of 2M urea with initial stages of denaturation

spinqualitylabelsall models 6ewn, resolution 2.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ewn is a 2 chain structure with sequence from Synechococcus vulcanus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: URE Gene: hspA (Synechococcus vulcanus) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Small heat shock proteins (sHSPs) belong to the superfamily of molecular chaperones. They prevent aggregation of partially unfolded or misfolded client proteins, providing protection to organisms under stress conditions. Here, we report the biophysical and structural characterization of a small heat shock protein (HspA) from a thermophilic cyanobacterium Thermosynechococcus vulcanus in the presence of 2M urea. HspA has been shown to be important for the protection of Photosystem II and the Phycobilisome antenna complex at elevated temperatures. Heterologously expressed HspA requires the presence of 1-2M urea to maintain its solubility at concentrations required for most characterization methods. Spectroscopic studies reveal the presence of the beta-sheet structure and intactness of the tertiary fold in HspA. In vitro assays show that the HspA maintains chaperone-like activity in protecting soluble proteins from thermal aggregation. Chromatography and electron microscopy show that the HspA exists as a mixture of oligomeric forms in the presence of 2M urea. HspA was successfully crystallized only in the presence of 2M urea. The crystal structure of HspA shows urea-induced loss of about 30% of the secondary structure without major alteration in the tertiary structure of the protein. The electron density maps reveal changes in the hydrogen bonding network which we attribute to the presence of urea. The crystal structure of HspA demonstrates a mixture of both direct interactions between urea and protein functionalities and interactions between urea and the surrounding solvent that indirectly affect the protein, which are in accordance with previously published studies. Biophysical and structural characterization of the small heat shock protein HspA from Thermosynechococcus vulcanus in 2 M urea.,Ghosh S, Salama F, Dines M, Lahav A, Adir N Biochim Biophys Acta Proteins Proteom. 2019 Apr;1867(4):442-452. doi:, 10.1016/j.bbapap.2018.12.011. Epub 2019 Jan 31. PMID:30711645 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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