A designed apoplastocyanin variant that shows reversible folding.
Plastocyanin, like many other metalloproteins, does not undergo reversible folding, which is thought to be due to an irreversible conformational change in the copper-binding site. Moreover, apoplastocyanin's ability to adopt a native tertiary structure is highly salt-dependent, and even in high salt, it has an irreversible thermal denaturation. Here, we report a designed apoplastocyanin variant, PCV, that is well folded and has reversible folding in both high and low salt conditions. This variant provides a tractable model for understanding and designing protein beta-sheets.
Division of Biology (Biochemistry and Molecular Biophysics option), California Institute of Technology, 1200 East California Blvd, Pasadena, CA 91125, USA.
Deepshikha
D
Datta
Stephen L
SL
Mayo
D001059:Apoproteins / Q000737:chemistry* / Q000235:genetics*; D001665:Binding Sites; D002942:Circular Dichroism; D003300:Copper / Q000378:metabolism; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D010940:Plant Proteins / Q000737:chemistry; D010970:Plastocyanin / Q000737:chemistry* / Q000235:genetics*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012492:Salts / Q000494:pharmacology; D013696:Temperature
D001059:Apoproteins; D010940:Plant Proteins; D012492:Salts; C040778:apoplastocyanin; D003300:Copper; D010970:Plastocyanin