1tq1

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Solution structure of At5g66040, a putative protein from Arabidosis Thaliana

Overview

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.

About this Structure

1TQ1 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

Solution structure of a single-domain thiosulfate sulfurtransferase from Arabidopsis thaliana., Cornilescu G, Vinarov DA, Tyler EM, Markley JL, Cornilescu CC, Protein Sci. 2006 Dec;15(12):2836-41. Epub 2006 Nov 6. PMID:17088324

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