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Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein

Center for Eukaryotic Structural Genomics, Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706-1544, USA

(RECEIVED November 16, 2004; FINAL REVISION December 21, 2004; ACCEPTED December 21, 2004)

The structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein, was determined by NMR spectroscopy. The structure is dominated by a -barrel sandwich. A two-stranded anti-parallel -sheet, which seals off one end of the -barrel, is flanked by two flexible loops rich in acidic amino acids. Although this fold often provides a ligand binding site, the structure did not reveal an appreciable cavity inside the -barrel. The three-dimensional structure of At3g04780.1-des15 provides an entry point for understanding its functional role and those of its mammalian homologs.

Keywords: structural genomics; Arabidopsis thaliana; NMR; TXNL_HUMAN ortholog

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.041246805.

Reprint requests to: John L. Markley, Center for Eukaryotic Structural Genomics, Department of Biochemistry, 433 Babcock Drive, University of Wisconsin-Madison, Madison, WI 53706-1544, USA; e-mail: markley{at}nmrfam.wisc.edu; fax: (608) 262-3759.

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