title: Utility of Synechocystis sp. PCC 6803 glutaredoxin A as a platform to study high-resolution mutagenesis of proteins.
abstract: Glutaredoxin from the cyanobacterium Synechocystis sp. PCC 6803 is a small protein, containing only 88 amino acids, that participates in a large number of redox reactions, serving both as an electron donor for enzyme-catalyzed reductions and as a regulator of diverse metabolic pathways. The crystal structures of glutaredoxins from several species have been solved, including the glutaredoxin A isoform from the cyanobacterium Synechocystis sp. PCC 6803. We have utilized the small size of Synechocystis glutaredoxin A and its propensity to form protein crystals that diffract to high resolution to explore a long-standing question in biochemistry; i.e., what are the effects of mutations on protein structure and function? Taking advantage of these properties, we have initiated a long-term educational project that would examine the structural and biochemical changes in glutaredoxin as a function of single-point mutational replacements. Here, we report some of the mutational effects that we have observed to date.
authors.affiliation: Department of Chemistry and Biochemistry, Texas Tech University Lubbock, TX, USA ; Center for Biotechnology and Genomics, Texas Tech University Lubbock, TX, USA.
authors.forename: David B
authors.initials: DB
authors.lastname: Knaff
authors.forename: Roger B
authors.initials: RB
authors.lastname: Sutton
keywords: educational platform; glutaredoxin A; mutagenesis; protein structure; synechocystis sp. PCC 6803; tertiary