2c9x

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Revision as of 18:01, 29 October 2007

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spinqualitylabelsall models 2c9x, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

SULFITE DEHYDROGENASE FROM STARKEYA NOVELLA Y236F MUTANT

Overview

The sulfite dehydrogenase from Starkeya novella is the only known, sulfite-oxidizing enzyme that forms a permanent heterodimeric complex, between a molybdenum and a heme c-containing subunit and can be, crystallized in an electron transfer competent conformation. Tyr236 is a, highly conserved active site residue in sulfite oxidoreductases and has, been shown to interact with a nearby arginine and a molybdenum-oxo ligand, that is involved in catalysis. We have created a Tyr236 to Phe, substitution in the SorAB sulfite dehydrogenase. The purified SDH(Y236F), protein has been characterized in terms of activity, structure, intramolecular electron transfer, and EPR properties. The substituted, protein exhibited reduced turnover rates and substrate affinity as well as, an altered reactivity ... [(full description)]

About this Structure

2C9X is a [Protein complex] structure of sequences from [Thiobacillus novellus] with SO4, MSS and HEC as [ligands]. Full crystallographic information is available from [OCA].

Reference

Kinetic and structural evidence for the importance of Tyr236 for the integrity of the Mo active site in a bacterial sulfite dehydrogenase., Kappler U, Bailey S, Feng C, Honeychurch MJ, Hanson GR, Bernhardt PV, Tollin G, Enemark JH, Biochemistry. 2006 Aug 15;45(32):9696-705. PMID:16893171

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