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Published online before print November 6, 2006
Protein Science, DOI: 10.1110/ps.062395206
 Copyright © 2006 The Protein Society
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PROTEIN STRUCTURE REPORT

Solution structure of a single-domain thiosulfate sulfurtransferase from Arabidopsis thaliana

Gabriel Cornilescu1, Dmitriy A. Vinarov2, Ejan M. Tyler2, John L. Markley1,2, and Claudia C. Cornilescu1,2

1 National Magnetic Resonance Facility at Madison, Biochemistry Department, University of Wisconsin–Madison, Madison, Wisconsin 53706-1544, USA
2 Center for Eukaryotic Structural Genomics, Biochemistry Department, University of Wisconsin–Madison, Madison, Wisconsin 53706-1544, USA

(RECEIVED June 12, 2006; FINAL REVISION September 12, 2006; ACCEPTED September 18, 2006)

We describe the three-dimensional structure of the product of Arabidopsis thaliana gene At5g66040.1 as determined by NMR spectroscopy. This protein is categorized as single-domain sulfurtransferase and is annotated as a senescence-associated protein (sen1-like protein) and ketoconazole resistance protein (http://arabidopsis.org/info/genefamily/STR_genefamily.html). The sequence of At5g66040.1 is virtually identical to that of a protein from Arabidopsis found by others to confer ketoconazole resistance in yeast. Comparison of the three-dimensional structure with those in the Protein Data Bank revealed that At5g66040.1 contains an additional mobile beta-hairpin not found in other rhodaneses that may function in binding specific substrates. This represents the first structure of a single-domain plant sulfurtransferase. The enzymatically active cysteine-containing domain belongs to the CDC25 class of phosphatases, sulfide dehydrogenases, and stress proteins such as senescence specific protein 1 in plants, PspE and GlpE in bacteria, and cyanide and arsenate resistance proteins. Versions of this domain that lack the active site cysteine are found in other proteins, such as phosphatases, ubiquitin hydrolases, and sulfuryltransferases.

Keywords: At5g66040.1; single-domain sulfurtransferase; rhodanese; CESG; Center for Eukaryotic Structural Genomics; NMR

Reprint requests to: Gabriel Cornilescu, National Magnetic Resonance Facility at Madison, Biochemistry Department, University of Wisconsin–Madison, Madison, Wisconsin 53706-1544, USA; e-mail: gabrielc{at}nmrfam.wisc.edu; fax: (608) 262-3759.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.062395206.


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