4MJB

Synechocystis sp. PCC 6803 glutaredoxin A-A79S

Summary for 4MJB

• Entry DOI: 10.2210/pdb4mjb/pdb
• Related: 3qmx 4MJA 4MJC 4MJE
• Descriptor: Probable glutaredoxin ssr2061, SULFATE ION (3 entities in total)
• Functional Keywords: thioredoxin fold, oxidation/reduction, electron transport
• Biological source: Synechocystis sp.
• Total number of polymer chains: 1
• Total formula weight: 11229.62

Authors

Sutton, R.B.,Knaff, D.B. (deposition date: 2013-09-03, release date: 2013-12-04, Last modification date: 2023-09-20)

Primary citation

Knaff, D.B.,Sutton, R.B.
Utility of Synechocystis sp. PCC 6803 glutaredoxin A as a platform to study high-resolution mutagenesis of proteins.
Front Plant Sci, 4:461-461, 2013

PubMed 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.

PubMed: 24298277
DOI: 10.3389/fpls.2013.00461

Experimental method

X-RAY DIFFRACTION (2.111 Å)